ID W6U7F1_ECHGR Unreviewed; 510 AA.
AC W6U7F1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Katanin p60 ATPase-containing subunit A-like 2 {ECO:0000256|HAMAP-Rule:MF_03025};
DE Short=Katanin p60 subunit A-like 2 {ECO:0000256|HAMAP-Rule:MF_03025};
DE EC=5.6.1.1 {ECO:0000256|HAMAP-Rule:MF_03025};
DE AltName: Full=p60 katanin-like 2 {ECO:0000256|HAMAP-Rule:MF_03025};
GN Name=KATNAL2 {ECO:0000256|HAMAP-Rule:MF_03025};
GN ORFNames=EGR_07975 {ECO:0000313|EMBL:EUB57158.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB57158.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB57158.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
CC -!- FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This
CC activity may promote rapid reorganization of cellular microtubule
CC arrays. {ECO:0000256|HAMAP-Rule:MF_03025}.
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_03025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
CC Rule:MF_03025}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03025}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03025}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03025}.
CC Note=Localizes within the cytoplasm, partially overlapping with
CC microtubules in interphase and to the mitotic spindle and spindle poles
CC during mitosis. {ECO:0000256|HAMAP-Rule:MF_03025}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. A-like 2 sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUB57158.1}.
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DR EMBL; APAU02000092; EUB57158.1; -; Genomic_DNA.
DR AlphaFoldDB; W6U7F1; -.
DR STRING; 6210.W6U7F1; -.
DR EnsemblMetazoa; XM_024497224.1; XP_024348354.1; GeneID_36343690.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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; 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 HAMAP; MF_03025; Katanin_p60_AL2; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027497; Katanin_p60_AL2.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF78; KATANIN P60 ATPASE-CONTAINING SUBUNIT A-LIKE 2; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08513; LisH; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50896; LISH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03025};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03025};
KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03025};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03025};
KW Microtubule {ECO:0000256|HAMAP-Rule:MF_03025};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03025};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT DOMAIN 263..406
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 85..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 271..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03025"
SQ SEQUENCE 510 AA; 57695 MW; 5336838E4F2DA127 CRC64;
MICTANRARE SDFNRLQSRK KNLILLVMNF LTEEGFVNTA ATFKNEANID FDVYSICDNI
DLDTILMEFE SFYFVKFSKY PRISRKKDAN HDERKQRKTF LPNINRGSGS NKSRMARSSS
TKIVKANEVL AKDDATNHEN CQPLQESLSE IVAEGRVLNK TKGNTPSIDY QTLLSNENNA
ICEGQSSQER ILKPLGLFAG YSPEWAELAQ AISRVSFIKD IYLQNPNIHW DDIVGLETAK
QLVKEAVVYP VSYPELFSGI LSPWKGLLLY GPPGTGKTLL AKAVATECKT TFFNISASSI
VSKWRGDSEK LVRVLFEMAR FHSPSTIFLD ELDSLMSQRG SDGGSTVGMG EHEGSRRMKT
ELLIQMDGLA KSDDLIFLLA ASNIPWELDH AMLRRLEKRI LVDLPNFEAR KRMFEKLLPP
KQKPSKTMIP QLTAQIDYAH MAEHKFIEHL LACLGILSTF FFCDPALLQT KLHFDPITSG
DVESAIRRTK PSGMAFSEKY RKWQEKFGSS
//