ID   KATL2_XENTR             Reviewed;         542 AA.
AC   A0JMA9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Katanin p60 ATPase-containing subunit A-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
DE            Short=Katanin p60 subunit A-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
DE            EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03025};
DE   AltName: Full=p60 katanin-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
GN   Name=katnal2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Oviduct;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This
CC       activity may promote rapid reorganization of cellular microtubule
CC       arrays. {ECO:0000255|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:0000255|HAMAP-Rule:MF_03025};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC       Rule:MF_03025}. Cytoplasm {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8IYT4}.
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:0000250|UniProtKB:Q8IYT4}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC       subfamily. A-like 2 sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03025}.
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DR   EMBL; BC125808; AAI25809.1; -; mRNA.
DR   RefSeq; NP_001090643.1; NM_001097174.1.
DR   AlphaFoldDB; A0JMA9; -.
DR   SMR; A0JMA9; -.
DR   STRING; 8364.ENSXETP00000061187; -.
DR   PaxDb; A0JMA9; -.
DR   PRIDE; A0JMA9; -.
DR   DNASU; 100036615; -.
DR   GeneID; 100036615; -.
DR   KEGG; xtr:100036615; -.
DR   CTD; 83473; -.
DR   Xenbase; XB-GENE-5827282; katnal2.
DR   eggNOG; KOG0738; Eukaryota.
DR   InParanoid; A0JMA9; -.
DR   OrthoDB; 787710at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; 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: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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03025; Katanin_p60_AL2; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027497; Katanin_p60_AL2.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF08513; LisH; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00667; LisH; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..542
FT                   /note="Katanin p60 ATPase-containing subunit A-like 2"
FT                   /id="PRO_0000333795"
FT   DOMAIN          25..57
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03025"
FT   REGION          94..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         298..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03025"
SQ   SEQUENCE   542 AA;  60918 MW;  170AC7FBB6D94D74 CRC64;
     MELSYQALRV ASQNREAEEL RTEARRKNLL ILIMHYLLQE GYMDSANSLE QETKISLRRF
     DVCDNVDLET ILMEYESYYY IKFQKYPKIT KKALDHDSRV QSKPRSAGKL RRAGSNSTQG
     LPRIAQQTVL HRPVSGSYFR THAHQKALSR ENSKQENGGN SPREASEIGL NVSAISKTSG
     EGGQTRRRQV IDFRSMIQDT IKGASQEIAL NSLNCNPDPS ERLIKPVGAF IGGNSEMREL
     AAVISRDIYL QNPNVRWDDI IGLDAAKRLV KEAVVYPIRY PQLFTGILSP WKGLLLYGPP
     GTGKTLLAKA VATECNTTFF NISASTIVSK WRGDSEKLVR VLFELARYHA PSTIFLDELE
     SVMSQRGTGP GGEHEGSRRM KTELLVQMDG LARSDDLVFV LAASNLPWEL DYAMLRRLEK
     RILVDLPSKE ARQAMIQHWL PPVSNSSGVE LRTDLDYSTL GAETDGYSGS DIRLVCKEAA
     MRPVRKIFDA LENHHSEHKN LPVISLDTVT TSDFLEVLAH TKPSAKSLAE KYAAWQKEFE
     SV