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Database: UniProt
Entry: A0A0B1TPW4_OESDE
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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
//
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