ID A0A914URX3_9BILA Unreviewed; 497 AA. AC A0A914URX3; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 27-MAR-2024, entry version 6. DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023}; DE Short=Katanin p60 subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023}; DE EC=5.6.1.1 {ECO:0000256|HAMAP-Rule:MF_03023}; DE AltName: Full=p60 katanin {ECO:0000256|HAMAP-Rule:MF_03023}; GN Name=KATNA1 {ECO:0000256|HAMAP-Rule:MF_03023}; OS Plectus sambesii. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Plectida; Plectina; OC Plectoidea; Plectidae; Plectus. OX NCBI_TaxID=2011161 {ECO:0000313|Proteomes:UP000887566, ECO:0000313|WBParaSite:PSAMB.scaffold11701size3184.g34339.t3}; RN [1] {ECO:0000313|WBParaSite:PSAMB.scaffold11701size3184.g34339.t3} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (NOV-2022) to UniProtKB. CC -!- FUNCTION: Catalytic subunit of a complex which severs microtubules in CC an ATP-dependent manner. Microtubule severing may promote rapid CC reorganization of cellular microtubule arrays and the release of CC microtubules from the centrosome following nucleation. CC {ECO:0000256|HAMAP-Rule:MF_03023}. CC -!- CATALYTIC ACTIVITY: CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) CC alpha/beta tubulin heterodimers.; EC=5.6.1.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03023}; CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by microtubules, CC which promote homooligomerization. ATP-dependent microtubule severing CC is stimulated by interaction with KATNB1. {ECO:0000256|HAMAP- CC Rule:MF_03023}. CC -!- SUBUNIT: Can homooligomerize into hexameric rings, which may be CC promoted by interaction with microtubules. Interacts with KATNB1, which CC may serve as a targeting subunit. {ECO:0000256|HAMAP-Rule:MF_03023}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle CC pole {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, CC spindle {ECO:0000256|HAMAP-Rule:MF_03023}. Note=Predominantly CC cytoplasmic. Also localized to the interphase centrosome and the CC mitotic spindle poles. Enhanced recruitment to the mitotic spindle CC poles requires microtubules and interaction with KATNB1. CC {ECO:0000256|HAMAP-Rule:MF_03023}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03023}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR WBParaSite; PSAMB.scaffold11701size3184.g34339.t3; PSAMB.scaffold11701size3184.g34339.t3; PSAMB.scaffold11701size3184.g34339. DR Proteomes; UP000887566; Unplaced. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule. DR GO; GO:0008568; F:microtubule severing ATPase activity; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_03023; Katanin_p60_A1; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR028596; KATNA1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015415; Spast_Vps4_C. DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23074:SF19; KATANIN P60 ATPASE-CONTAINING SUBUNIT A1; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF09336; Vps4_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03023}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_03023}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_03023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}; KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03023}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03023}; KW Microtubule {ECO:0000256|HAMAP-Rule:MF_03023}; KW Mitosis {ECO:0000256|HAMAP-Rule:MF_03023}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03023}; Reference proteome {ECO:0000313|Proteomes:UP000887566}. FT DOMAIN 249..389 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 43..193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 179..193 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 257..264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023" SQ SEQUENCE 497 AA; 55090 MW; 9BF5D8A006F261A0 CRC64; MPLLSDQPQR KQEWLNAREV LQRELDDVKK VMAIVTDLRS LPAGGGGRLD DERNDFSPSD FFNDYDPPRD PDVWAPAPPL PRQYTSRTTT TARGGTSGMS RTRGGSTSNL MRRGTSNEQT RGGRMGSNNA MRKSNSQSGL NSAPKRANST GRLNNSAAGK DTREKGSDGS VDSKNVLNDC LPQEEDENRF ESSGYDKDLV DTIERDILVR DLNVKWTDIA GLEGAKKLLE EAVILPTLIP EFFKGIRRPW RGVCMVGPPG TGKTLLAKAV ATECKTTFFS VSSATLTSKY RGDSEKLVRL LFEMARFHAP STIFIDEIDS VCSRRGGETE HEASRRVKSE LLIQMDGCGS DAEDSAKSVM VLAATNFPWD LDEALRRRLE KRIYIPLPDE GGRLKLLELA LRDVSIAPDV ELPGVAKRLE GYSGADITSV CRDAAMMSMR RRIAGLNPDE IRALPQNEFD LPITNEDFDE AIRKTSPSVS DDDLDKFKRW MDEFGAS //