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Database: UniProt
Entry: B0X288_CULQU
LinkDB: B0X288_CULQU
Original site: B0X288_CULQU 
ID   B0X288_CULQU            Unreviewed;       543 AA.
AC   B0X288;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=microtubule-severing ATPase {ECO:0000256|ARBA:ARBA00038871};
DE            EC=5.6.1.1 {ECO:0000256|ARBA:ARBA00038871};
GN   Name=6046584 {ECO:0000313|EnsemblMetazoa:CPIJ013667-PA};
GN   ORFNames=CpipJ_CPIJ013667 {ECO:0000313|EMBL:EDS39111.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS39111.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS39111.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ013667-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ013667-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
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; DS232283; EDS39111.1; -; Genomic_DNA.
DR   RefSeq; XP_001863760.1; XM_001863725.1.
DR   AlphaFoldDB; B0X288; -.
DR   STRING; 7176.B0X288; -.
DR   EnsemblMetazoa; CPIJ013667-RA; CPIJ013667-PA; CPIJ013667.
DR   KEGG; cqu:CpipJ_CPIJ013667; -.
DR   VEuPathDB; VectorBase:CPIJ013667; -.
DR   VEuPathDB; VectorBase:CQUJHB018481; -.
DR   eggNOG; KOG0740; Eukaryota.
DR   HOGENOM; CLU_000688_21_2_1; -.
DR   InParanoid; B0X288; -.
DR   OMA; LCQEAIW; -.
DR   OrthoDB; 276256at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
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   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:UniProt.
DR   CDD; cd19524; RecA-like_spastin; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   InterPro; IPR015415; Spast_Vps4_C.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF86; SPASTIN; 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|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|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT   DOMAIN          300..437
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          35..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  58203 MW;  3B0F0A19C596A2A0 CRC64;
     MESSECMLEA NKLEISEAHK LQRSNTFTLS VGQPTVLPTA QPARPATSYA PTTTTTTVKR
     AQFKVPHPAK GALARPATAG RGQQQQQENR VMSYGDSNGG SGRNAPEPEA SGRKLTVGYK
     RPGNLGVMNK SQTLPRSMGG SRTTPTGGSG AAGTGYGVGP ATAGGAPGCT AGGGMPKIVP
     KPAATPPAIR RQFSIPSGSP IRKASNGYGH SGGKNTPPRS KTPLGTAPSN NQSGQQQQQQ
     ITVKGVEPKL VQIIMDEIVE GGAKVEWQDI AGQEVAKQAL QEMVILPSVR PELFTGLRTP
     AKGLLLFGPP GNGKTLLARA VATECSATFF SISAATLTSK YVGDGEKLVR ALFSVAREMQ
     PAIIFIDEVD SLLSERSSGE HEATRRLKTE FLVQFDGLPA NSEADKIVVM AATNRPQELD
     EAALRRFPKR VYVTLPDLDT RELLLRRLLE KQNSPLDDAD LKRLAMLTEG YSGSDLTALA
     KDAALEPIRE LNVEQVKHMD PTKLRSIRES DFHNSLKRIR RSVAPHSLAA YEKWLQDFGD
     VTL
//
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