ID A0A1X0NYV7_9TRYP Unreviewed; 564 AA. AC A0A1X0NYV7; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 29-SEP-2021, entry version 18. DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023}; DE Short=Katanin p60 subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023}; DE EC=5.6.1.1 {ECO:0000256|HAMAP-Rule:MF_03023}; DE AltName: Full=p60 katanin {ECO:0000256|HAMAP-Rule:MF_03023}; GN Name=KATNA1 {ECO:0000256|HAMAP-Rule:MF_03023}; GN ORFNames=TM35_000113150 {ECO:0000313|EMBL:ORC89781.1}; OS Trypanosoma theileri. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC89781.1, ECO:0000313|Proteomes:UP000192257}; RN [1] {ECO:0000313|EMBL:ORC89781.1, ECO:0000313|Proteomes:UP000192257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC89781.1}; RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P., RA Matthews J., Matthews K., Carrington M.; RT "An alternative strategy for trypanosome survival in the mammalian RT bloodstream revealed through genome and transcriptome analysis of the RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Severs microtubules in an ATP-dependent manner. Microtubule CC severing may promote rapid reorganization of cellular microtubule CC arrays. {ECO:0000256|HAMAP-Rule:MF_03023}. CC -!- CATALYTIC ACTIVITY: CC Reaction=n ATP + n H(2)O + 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_03023}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP- CC Rule:MF_03023}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03023}. 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:ORC89781.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NBCO01000011; ORC89781.1; -; Genomic_DNA. DR VEuPathDB; TriTrypDB:TM35_000113150; -. DR OrthoDB; 717356at2759; -. DR Proteomes; UP000192257; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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 Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_03023; Katanin_p60_A1; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR028596; KATNA1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015415; Vps4_C. 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; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03023}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}; KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03023}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03023}; KW Microtubule {ECO:0000256|HAMAP-Rule:MF_03023}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03023}; Reference proteome {ECO:0000313|Proteomes:UP000192257}. FT DOMAIN 312..449 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 320..327 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023" FT REGION 96..249 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 96..135 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 204..244 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 564 AA; 61971 MW; C2592586B355B470 CRC64; MCDLFTIVSS SEKSLRLARR YALESNYDVA VAFYTGIDKD LTNCMQCRSD GSQSGKNGSG DLSDVALLRE KVAEECVLVR AIQAELKALI NPSSAVQLDR PPQESNAETT TAPSRAATTR PLRRTTVTNT NGANPVAAAR PAVMSVPPPM STAARNEALY GDPDRFGPPR LKTPLRNSSP LARRRPVGGS LRAASPPRST RPKAALPLQT QSQQTLRAGR TPAASSSAAV SSTNNNTTSR PRRQGARATL PRFVARPGEE ELVSLIEADM HVGPLAVSWD DVAGLSAAKG LLEEAVVYPV LMPDYYTGIR RPWKGVLLYG PPGTGKTMLA KAVASECNTT FFNISPATLT SKWRGDSEKL IRVLFEMARY YAPSTIFIDE IDSLCGQRGD GGEHEASRRA KGTLLAQMDG VGVDPGKIVM VLGATNHPWS IDEAMRRRLE KRIYIPLPDF NDRLELFRIN TKTLKLSPDV DFTKLSKILE GRYYSCADIT NLVRDAAMMT MRRFMEETDK TELKRRAAEI GKLVAEQPTT MKDFLDAVKN VPSSINVDQI TRFEKWKKEF ETNL //