ID A0A078B8C4_STYLE Unreviewed; 580 AA.
AC A0A078B8C4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=Contig19289.g20447 {ECO:0000313|EMBL:CDW89542.1};
GN Synonyms=KATNA1 {ECO:0000256|HAMAP-Rule:MF_03023};
GN ORFNames=STYLEM_18675 {ECO:0000313|EMBL:CDW89542.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW89542.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW89542.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW89542.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Severs microtubules in an ATP-dependent manner. Microtubule
CC severing may promote rapid reorganization of cellular microtubule
CC arrays. {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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
CC 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; CCKQ01017644; CDW89542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078B8C4; -.
DR EnsemblProtists; CDW89542; CDW89542; STYLEM_18675.
DR InParanoid; A0A078B8C4; -.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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: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}; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03023}; Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT DOMAIN 321..470
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
SQ SEQUENCE 580 AA; 64890 MW; 90AF01B79DCDAB2B CRC64;
MVAEQINREY AMTNETLQIK KSFSVNINGL ITTQFIQNGF GTGLQNRKNN ALDKLPVNIM
TADQNMILNP IVPLPTQKRM PNFDRLGGQP FAHHTSNPDN YFGNDIDDQM GNQHMSYVQR
RNKSQFQQHN ANSRDQDYGS SNDPDIWEPP TPPKYGVPQP RGIMGGGMGM GMGGMPPGIP
QSNWGQQPRR QPQPQQRKPP INSVTRPPQG PQGGAVAGVK NKQNLLDKNR NYTKPWLSGA
QSGENQKDVK PDQNSFLYTM YPDGNGPDSE LIQMLERDVI DKNPQVSFND IAELDDAKKI
LQEAVLLPIL MPQYFKGIRR PWKGVLMFGP PGTGKTMLAK AVATQGKTTF FNITSSSISS
KWKGESEKLV RILFEMARFY APTTIFMDEI DAIAGARGGN EHEANRRVKA ELLIQMDGVA
VVSSAGANEN QAEGERMKNV MVLAATNRPW DLDEAFRRRL EKRIYIPLPN ELGRKQLFEI
NLKGIKMAED TNLDQLVKKT KGYSGADISN VCRDAAMMPM RKKILEGKLS FEQIASLKHD
EIDIPITQSD FLDALKNISK SVSKESLDDY AKWMAEFGCV
//
