ID A0A0B1TPW4_OESDE Unreviewed; 420 AA.
AC A0A0B1TPW4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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};
GN ORFNames=OESDEN_00724 {ECO:0000313|EMBL:KHJ99299.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ99299.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ99299.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ99299.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN549228; KHJ99299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1TPW4; -.
DR Proteomes; UP000053660; Unassembled WGS sequence.
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:UniProtKB-EC.
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:UP000053660}.
FT DOMAIN 174..312
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 42..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
SQ SEQUENCE 420 AA; 46789 MW; 9904D88E743A79BF CRC64;
MDFSSIDEIV ERARKSDDYK VVDSSYKEAI SELEAISASL GAAEKKQVRH SRNAEANETI
TVKKPVKKSS SQNALAEKKQ KQNATATVTG TSTAPEAPPA ETTTNPSEDK QKDEFIPRGY
CPDLVEAIEQ TMTRNGTEVC WDDIAGLEGP KELFKQTIVL PALMPNFFKG IRRPWRGVCM
VGPPGTGKTL LAKAVATECQ TTFFAVSCGD LASKWRGDSE KMIKLLFEMA RHFAPSTIFI
DEIDTIGSQR GQANEHEASR RVKSQLLVEM DGFNKEEDGK RVLVLAATNF PWMLDEALRR
RFEQRIYIPL PDQPARLSLL RSSLKEVRVD DDVDLDVFAT QLEGYSGADI TNVCRKAALM
GVKRLTRTLT PAEIAKLSPE ELDLPVTWQD LQEALGDTNP SVCEENIRQY TAWMEKYGST
//