ID   SPAST_CAEBR             Reviewed;         542 AA.
AC   A8XV40;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Probable spastin homolog spas-1;
DE            EC=5.6.1.1;
GN   Name=spas-1; ORFNames=CBG19220;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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}. Note=Localized to the perinuclear
CC       region of the cytoplasm in early embryos. Present in the cytoskeletal
CC       fraction. {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; HE601047; CAP36507.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XV40; -.
DR   SMR; A8XV40; -.
DR   STRING; 6238.CBG19220; -.
DR   PRIDE; A8XV40; -.
DR   WormBase; CBG19220a; CBP39759; WBGene00038478; Cbr-spas-1.
DR   eggNOG; KOG0740; Eukaryota.
DR   HOGENOM; CLU_000688_21_12_1; -.
DR   InParanoid; A8XV40; -.
DR   OMA; CSTYERV; -.
DR   OrthoDB; 1176820at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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; Coiled coil; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..542
FT                   /note="Probable spastin homolog spas-1"
FT                   /id="PRO_0000367131"
FT   REGION          131..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          29..66
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        134..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         309..316
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   542 AA;  60735 MW;  38AD69F081E85355 CRC64;
     MFAFSKAPAG CSTYERVTQK FQDGSNKLRA AIEMDELTKQ NGTINEKLQT AELYKQARQM
     LKEANEFNIM DIPESKRSEV REKREKTLNL EKSAQDRLIK ICNEVDPNMK RASTAADPCR
     AARITPRNTR ATVPGDKKVS KVKQTEKAPH VCSRGDRCGA HQPPPEKKST PLKPVNQIRT
     RVKENKNPIG VQQQVFSFIL SCCMRRNCRR PHYLFPCMIS LKMNYFKFQA TLPNQLNTVN
     RSNLLKGVDK AIGERLLDEI LDSTGVRMDD VAGCHSAKAT LEEAVILPAL NPNLFSGLRQ
     PVKGILLFGP PGNGKTLLAK AVAGESKQMF FNISASSLTS KWVGDSEKTI RGLFQIARNG
     QPSIIFIDEI DSILCERSEK DAEVSRRMKT EFLVQFDGAT SSPDDRILVI GATNRPYELD
     DAVLRRFPKR IMLNLPDTEA RKELITNTLK KHDMMDGLSS SDIRYIASNT SGFSNSDLVA
     LCKEAAMVPV REIHRSKLSV TDGDKIRKIR ASDFDTALRT IRPSTSDRIL SKLSDFSRNF
     GC