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5WC1

katanin AAA ATPase domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0000212biological_processmeiotic spindle organization
A0000226biological_processmicrotubule cytoskeleton organization
A0000785cellular_componentchromatin
A0000922cellular_componentspindle pole
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007019biological_processmicrotubule depolymerization
A0007143biological_processfemale meiotic nuclear division
A0008017molecular_functionmicrotubule binding
A0008352cellular_componentkatanin complex
A0008568molecular_functionmicrotubule severing ATPase activity
A0009792biological_processembryo development ending in birth or egg hatching
A0015630cellular_componentmicrotubule cytoskeleton
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0019903molecular_functionprotein phosphatase binding
A0042802molecular_functionidentical protein binding
A0051013biological_processmicrotubule severing
A0051229biological_processmeiotic spindle disassembly
A0051301biological_processcell division
A0051321biological_processmeiotic cell cycle
A0060090molecular_functionmolecular adaptor activity
A0071688biological_processstriated muscle myosin thick filament assembly
A0072687cellular_componentmeiotic spindle
A0090619cellular_componentmeiotic spindle pole
A0090736molecular_functionMATH domain binding
A1902120biological_processnegative regulation of meiotic spindle elongation
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 501
ChainResidue
AGLY236
ATHR237
AGLY238
ALYS239
ATHR240

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 502
ChainResidue
AILE196
AGLY197
ALYS369

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues20
DetailsAAA AAA-protein family signature. VfVLaATNipweLDeALrrR
ChainResidueDetails
AVAL333-ARG352

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:28783150, ECO:0007744|PDB:5WC0, ECO:0007744|PDB:5WCB
ChainResidueDetails
AGLY233

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:28783150, ECO:0007744|PDB:5WC0, ECO:0007744|PDB:5WCB
ChainResidueDetails
AARG351

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by mbk-2 => ECO:0000269|PubMed:16338136
ChainResidueDetails
ASER92

223532

PDB entries from 2024-08-07

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