ID   SPAST_BRUMA             Reviewed;         454 AA.
AC   A8QFF6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable spastin homolog Bm1_53365;
DE            EC=5.6.1.1;
GN   ORFNames=Bm1_53365;
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17885136; DOI=10.1126/science.1145406;
RA   Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA   Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA   Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA   Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA   Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J.,
RA   Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA   Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W.,
RA   Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA   McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA   Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA   Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA   Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA   Blaxter M.L., Scott A.L.;
RT   "Draft genome of the filarial nematode parasite Brugia malayi.";
RL   Science 317:1756-1760(2007).
CC   -!- FUNCTION: Severs microtubules, probably in an ATP-dependent fashion.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homohexamer. The homohexamer is stabilized by ATP-binding. The
CC       homohexamer may adopt a ring conformation through which microtubules
CC       pass prior to being severed. Interacts with microtubules (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       perinuclear region {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved MIT domain, which is one of the features
CC       of the spastin family. {ECO:0000305}.
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DR   EMBL; DS239470; EDP29011.1; -; Genomic_DNA.
DR   RefSeq; XP_001902141.1; XM_001902106.1.
DR   AlphaFoldDB; A8QFF6; -.
DR   SMR; A8QFF6; -.
DR   STRING; 6279.A8QFF6; -.
DR   PRIDE; A8QFF6; -.
DR   EnsemblMetazoa; Bm2335b.1; Bm2335b.1; WBGene00222596.
DR   GeneID; 6105557; -.
DR   KEGG; bmy:BM_BM2335; -.
DR   WBParaSite; Bm2335b.1; Bm2335b.1; WBGene00222596.
DR   CTD; 6105557; -.
DR   WormBase; Bm2335a; BM25701; WBGene00222596; Bma-spas-1.
DR   HOGENOM; CLU_000688_21_12_1; -.
DR   InParanoid; A8QFF6; -.
DR   OrthoDB; 1176820at2759; -.
DR   Proteomes; UP000006672; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
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:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..454
FT                   /note="Probable spastin homolog Bm1_53365"
FT                   /id="PRO_0000367130"
FT   BINDING         218..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   454 AA;  51150 MW;  CC1366536E4FB80A CRC64;
     MLHPQKLEQQ NYETFNKAYL KSKQLVTEGV SIDEISSNND EQRKRIAMEK YRMGIEYFEK
     ALKISPDKVY PEKRSEVITH REAMKRNLEA TKGRLSDLEK MFPSKGNRNL QHRPVQFVSP
     SISKPQTAQL SSRPISSEKK NINYSNARTR SNLLKGVDDK FGGPLLNEIL NQDDVKMSDI
     IGAETAKRAL EETVILPTVN PSLFSGLRQP AQGILLFGPP GNGKTLLARA VAGECGSTMF
     LNVSAASLTS KWVGDAEKIV RALFQIARNG QPTIIFIDEI DSILCERNEK ETEVSRRMKT
     EFLIQMDGML SSKDDRLLVI GATNRPEELD SAILRRFPKR ILIDVPNAAA RLKLIMSLLE
     KTKTSFDLGL TQRQILAEWT HGYSNSDLVA LCREAAMVPI RDLSRKDIKN LVSTELRPIT
     LRDFEIAMKA IKPSTNERML QKLRKYAATA GQSD