ID A0A024TWQ4_9STRA Unreviewed; 358 AA.
AC A0A024TWQ4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=microtubule-severing ATPase {ECO:0000256|ARBA:ARBA00038871};
DE EC=5.6.1.1 {ECO:0000256|ARBA:ARBA00038871};
GN ORFNames=H310_08585 {ECO:0000313|EMBL:ETV98423.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV98423.1};
RN [1] {ECO:0000313|EMBL:ETV98423.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV98423.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00036378};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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DR EMBL; KI913969; ETV98423.1; -; Genomic_DNA.
DR RefSeq; XP_008872620.1; XM_008874398.1.
DR AlphaFoldDB; A0A024TWQ4; -.
DR EnsemblFungi; H310_08585-t26_2; H310_08585-t26_2-p1; H310_08585.
DR EnsemblProtists; ETV98423; ETV98423; H310_08585.
DR GeneID; 20085635; -.
DR VEuPathDB; FungiDB:H310_08585; -.
DR OrthoDB; 276256at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 CDD; cd19509; RecA-like_VPS4-like; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF86; SPASTIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF04212; MIT; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF116846; MIT domain; 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|RuleBase:RU003651};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651}.
FT DOMAIN 171..307
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 96..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39237 MW; 8A88BFB2BADF1CEE CRC64;
MFLFSFMKSS KAATEELPAP VPSKKESNSS LHDLAALAIA ADERGDVKAA IDLYVQVIER
MLKQVKDVHD PEMQRDMRRK IQGFMARAET LKAVASPAGR VHQPHAPSRP HSKTRATNPT
LAHAVLDDVL ETAPDVRWGD IAGLDDAKQM LQEAVVLPLL RPDLFTGLRA APKGALLFGP
PGTGKTMLAK AVATESHATF FSVTASTLTS KWVGEGEKLV RALFDMAREL QPSVIFLDEI
DSLLSIRSAG EHDAARRLKN EFLIQLDGVG SSSEDRILVL GATNLPHDLD EAIVRRLEKR
VYVPLPDEAA RKYLIGHLLR PHKHSLTDRD IAAVAAATDQ YVVCFVRRGG GCTRCHAW
//
