ID A0A369SB15_9METZ Unreviewed; 557 AA.
AC A0A369SB15;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=TrispH2_003907 {ECO:0000313|EMBL:RDD43721.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD43721.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD43721.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD43721.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD43721.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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:RDD43721.1}.
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DR EMBL; NOWV01000034; RDD43721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369SB15; -.
DR STRING; 287889.A0A369SB15; -.
DR Proteomes; UP000253843; 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; 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 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; PF17862; AAA_lid_3; 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:UP000253843}.
FT DOMAIN 296..434
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 103..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03025"
SQ SEQUENCE 557 AA; 62520 MW; 6C421E168EE7F432 CRC64;
MTHELSYMQI KTANQVREAE EQKIEQRRKS LLVLILQYLN DEGYVQSAKC LETESSTTLN
KFQVCDNVDL PTILQEYESY YYVKFNKYPK IIKKVSAEKQ AQFHSQNSSI SKNKGRSNPL
PKIPPSRRPS DDTAAREPRD NNSQNRSLSA SSVSTKKNST NKKESVSTPE AKVESDLGLT
GVAVQSTSST SKGQQKLSKT TDSTTNLSNQ AKSIANTRKS DQYDPSERLL KPISTMIGYS
NEMKELVGII SREIYLHNPN VRWSDIIGLE KPIKLVKESV VYPIKYPQLF SGILSPWKGL
LLYGPPGTGK TMLAKAVATE CNTTFFNISA SSIVSKWRGD SEKLVRVLFE LARHHAPSTI
FLDEIESLMG QRGSAGISEH EGSRRMKTEL LIQMDGLARS KDLVFVLATS NIPWELDLAM
LRRLEKRILI DLPTCQARKA MFRYHLPPVI QMQEEGLQLR TEVDYEMVAE ATDGYSGSDI
HLVCKEAAMR SIRKIFDVLE SIQLDGESSA TQLSKALSID PITTQNVFEA LKDTKPSASG
FKDKYKAWQA QFESTTS
//
