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Database: UniProt
Entry: B9GEI4_POPTR
LinkDB: B9GEI4_POPTR
Original site: B9GEI4_POPTR 
ID   B9GEI4_POPTR            Unreviewed;       531 AA.
AC   B9GEI4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 2.
DT   27-MAR-2024, entry version 94.
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=POPTR_001G176900 {ECO:0000313|EMBL:PNT55147.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT55147.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT55147.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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 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_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}.
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DR   EMBL; CM009290; PNT55147.1; -; Genomic_DNA.
DR   RefSeq; XP_002299621.2; XM_002299585.2.
DR   AlphaFoldDB; B9GEI4; -.
DR   STRING; 3694.B9GEI4; -.
DR   GeneID; 7490977; -.
DR   KEGG; pop:7490977; -.
DR   eggNOG; KOG0738; Eukaryota.
DR   HOGENOM; CLU_000688_21_1_1; -.
DR   InParanoid; B9GEI4; -.
DR   OMA; RDASMML; -.
DR   OrthoDB; 276256at2759; -.
DR   Proteomes; UP000006729; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd21748; Kp60-NTD; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 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; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR028596; KATNA1.
DR   InterPro; IPR048611; KATNA1_MIT.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF19; KATANIN P60 ATPASE-CONTAINING SUBUNIT A1; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF21126; KATNA1_MIT; 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|HAMAP-Rule:MF_03023,
KW   ECO:0000256|RuleBase:RU003651};
KW   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|HAMAP-Rule:MF_03023,
KW   ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006729}.
FT   DOMAIN          279..422
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          91..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         287..294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
SQ   SEQUENCE   531 AA;  58200 MW;  442EB4585CDE4B32 CRC64;
     MVGSASGSST ATATAALSGL QDHLKLAREY ALGGLYDTSI IFFDGAIAQI IKHLTTLDDP
     LIRTKWMNLK KSLSEETQAV KELDAERRAL KEAPASRRVA SPPIHPKSSF LFQPLDEYPS
     PSAAPIDDPD VWRPPSRDTA SRRPARSAQA GIRKSPQDGV WARGASTRTS TTGRGAKTGG
     SGRVNSGVRA STTGKRGTVT GKPGKGDSAN GDAEDGKKRP QYEGPDPDLA EMLERDVLET
     SPGVRWDDVA GLSEAKRLLE EAVVLPLWMP EYFQGIRRPW KGVLMFGPPG TGKTLLAKAV
     ATECGTTFFN VSSATLASKW RGESERMVRC LFDLARAYAP STIFIDEIDS LCNARGASGE
     HESSRRVKSE LLVQVDGVNN SSTGEDGSRK IVMVLAATNF PWDIDEALRR RLEKRIYIPL
     PKFESRKELI RINLKTVEVA TDVNVDEVAR RTEGYSGDDL TNVCRDASLN GMRRKIAGKT
     RDEIKNMPKD EISKDPVAMC DFEEALRKVQ RSVSQTDIEK HEKWFSEFGS A
//
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