ID A0A0D9VQF6_9ORYZ Unreviewed; 680 AA.
AC A0A0D9VQF6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 homolog {ECO:0000256|HAMAP-Rule:MF_03022};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR03G05640.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR03G05640.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR03G05640.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR03G05640.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: May participate in a complex which severs microtubules in an
CC ATP-dependent manner. Microtubule severing may promote rapid
CC reorganization of cellular microtubule arrays. {ECO:0000256|HAMAP-
CC Rule:MF_03022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
CC Rule:MF_03022}.
CC -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03022}.
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DR AlphaFoldDB; A0A0D9VQF6; -.
DR STRING; 77586.A0A0D9VQF6; -.
DR EnsemblPlants; LPERR03G05640.1; LPERR03G05640.1; LPERR03G05640.
DR Gramene; LPERR03G05640.1; LPERR03G05640.1; LPERR03G05640.
DR eggNOG; KOG0267; Eukaryota.
DR Proteomes; UP000032180; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0008352; C:katanin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03022; Katanin_p80_B1; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR028021; Katanin_C-terminal.
DR InterPro; IPR026962; KTNB1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19845; KATANIN P80 SUBUNIT; 1.
DR PANTHER; PTHR19845:SF14; KATANIN P80 WD40 REPEAT-CONTAINING SUBUNIT B1 HOMOLOG; 1.
DR Pfam; PF13925; Katanin_con80; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03022};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|HAMAP-
KW Rule:MF_03022}; Microtubule {ECO:0000256|HAMAP-Rule:MF_03022};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 51..93
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 94..135
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 136..177
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 178..219
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 220..261
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 545..670
FT /note="Katanin p80 subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13925"
FT REGION 380..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 74875 MW; C9050B86838E5F66 CRC64;
MAQGVWMSST NVLHRFSSAG AHAEQRKTTK SVFGNLREEQ RKMTKSVSEE FVAHASDVNC
VKVGKRTSRI LITGGEDKKV NVWAIGKPSA VLSLSGLTSP VDSVSFDSSE VMIGAGASSG
TIKIWDVEEA KVIRTFTGHR SSCASLDFHP FGEFFASGSS DTNMKIWDMR KKGCIHTYKG
HTRRIDVLRF TPDGRWIVSG GSDNSVKIWD LTAGKLLHDF KMHEGPINCL DFHPHEFLLA
TGSADKTVKF WDLETFELIG SSGPENSREY FEPASVVRSM TFNKDGKSLF CGLHESLKVL
SWEPIICHDM VDIGWSTLGD LIVHEGKLVG CSYNQSCVGV WIVDLMKIEP YAVSNAEEYL
NGSVKRSIQA DNSISSVLGR LSVSSSPDNE TSSSTLHKPS KMSASKEVPV PASSAMTQKL
PKAPVTSNHQ LTRSDSVPVL SPRVRLNPKF FDDQKRQIDY VVPVTAPRAH SKVDPRRSSL
PSVAPTNRPR SKTSAFSSEG SSFIPVAATR HSPKRLRSSV AGEQRASAGD EDNIADLMEN
HQEFIHAVKS RLTKLEVSAD IINVLMENTN SITLDICTSV LRLASSVLES SYDSHLKVAL
EMIIKLVKSF GAIISSTLSF TPVGVDIEAE QRFQRCNLCF QELVKVHSVL FTLTRRQGEV
GRSAQELSLF LQDIFQQSSR
//
