ID D8LRZ3_ECTSI Unreviewed; 778 AA.
AC D8LRZ3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=Esi_0007_0029 {ECO:0000313|EMBL:CBN73777.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN73777.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN73777.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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; FN648926; CBN73777.1; -; Genomic_DNA.
DR AlphaFoldDB; D8LRZ3; -.
DR STRING; 2880.D8LRZ3; -.
DR EnsemblProtists; CBN73777; CBN73777; Esi_0007_0029.
DR eggNOG; KOG0738; Eukaryota.
DR InParanoid; D8LRZ3; -.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000002630; Chromosome LG06.
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 CDD; cd21748; Kp60-NTD; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 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; IPR048611; KATNA1_MIT.
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; PF21126; KATNA1_MIT; 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:UP000002630}.
FT DOMAIN 485..662
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 87..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 493..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
SQ SEQUENCE 778 AA; 80552 MW; 4C6B21669A09D105 CRC64;
MQQPTLPADV VTLPETLTKF REHALKGNYA LAQRYHEQGT AAIESLVAGM DGDDSRRAKW
TGLATELDAE LKIVKDIVKE LARTVSLAGS SGPTEERRSS GGVAFTAGEP GDLAVRVSSR
ENQHQQHHSR GSIIDGRNRQ NIGGAVDRLD LGLGSLAIDP DGPVATDDPD VWPPPTPDPS
RGGAVLHQAG AAAGGGPGSG LSPGPRFGGG VASSKLVRRE VAAAALASDM ARQQLPAWAR
AGTPAAGNGS RAGSGRERRG SSGGGGGGGA GVGGGLPRKD SVVRGRMVIG GAGGAGGGGG
GQMGNRRNSR DQVKVDPKAR RESKDTGAAG AGPRRRRSSF GGGVGGGAAG GAESRVAGSV
DPARAAGGGS RRQQQQHGAG AAAPTSAGRA EGREGRRGWA PEAKRQGSPP AVTGPAQQPR
YSDLAREEGW ADRELIESLE RDIVERGVSV TWDQIADLKD AKQLLQEAVV LPLWMPDYFK
GIRRPWKGVL MFGPPGTGKT MLAKAVAAEC KTTFFNVSAS TLGSKYRGES EKMVRVLFEM
ARYYAPSTIF FDEIDSLAGS RGSDGEHEAS RRVKTELMVQ MDGVTGGGGG DGSSPGDQGS
DEAGGGGGGG GSGDGGGDGA SGHGGGASSK TVIVLAATNT PWSLDEALRR RLEKRIYIPL
PTEVGRKELF RINLGDVEVD DDVDLDALAG LTDGYSGADV AIVCRDAAMM SVRRVMKGAL
ERGLSGPEIQ KHVMEMKDEL AAAVTMEDFR SSLRKVSKSV GQADLDKYDE WMKEFGSA
//
