ID A0A0B2SN21_GLYSO Unreviewed; 834 AA.
AC A0A0B2SN21;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 homolog {ECO:0000256|HAMAP-Rule:MF_03022};
GN ORFNames=glysoja_041147 {ECO:0000313|EMBL:KHN46320.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN46320.1};
RN [1] {ECO:0000313|EMBL:KHN46320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN46320.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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; KN641387; KHN46320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2SN21; -.
DR Proteomes; UP000053555; Unassembled WGS sequence.
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; 2.
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:SF15; KATANIN P80 WD40 REPEAT-CONTAINING SUBUNIT B1 HOMOLOG KTN80.2; 1.
DR Pfam; PF13925; Katanin_con80; 1.
DR Pfam; PF00400; WD40; 6.
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; 5.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 31..73
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 74..115
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 116..157
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 158..199
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 200..241
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 673..831
FT /note="Katanin p80 subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13925"
FT REGION 576..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 92602 MW; 265A2768FD8C308A CRC64;
MAKTGYKLRI LFYIYKFCAS ENAFCCNVEE FAAHSGNVNC LKLGRKANRL FITGGDDHSV
NLWMIGKPTS LMSLCGHTSS VESVTFDSAE VLILSGASSG VIKLWDLEEA KMVRTLTGHR
LNCTAVEFHP FGEFFASGSL DTNLNIWDIR KKGCIQTYKG HSQGISTIKF SPDGRWVVSG
GFDNVVKVWD LTGGKLLHDF KFHEGHIRSL DFHPLEFLMA TGSADRTVKF WDLETFELIG
STRHEVSGVR SIAFHPDGQI LFAGLEDSLK VYSWEPVICH DAVDMGWTTL GDLCIHDGML
LGCSFYSNSV GVWVSDISLI EPYNGGLETE KKESTKQKLS LQGRQMEKVE AGVGPAFGLC
SMSADNESKE IKNIYIDSSG GNPDTLIRSR SYNSPKVDLP EESKEMLNWS PATRAHAKQN
EQTLRKSYIM PNFVPRDIVN GKNSATFSKT KPGMLLKPVH VQGASTDILD VDGFSSDLDS
RTFCDTGSKS DSAKDPNFQM KLGSQNEVRE SIEDKHPIKS VTEKFEKTLT PDRFSDQDKC
NQSSPYSKEM SPVKYVNGVA VLQGRTRSLV ERFERRERTP TDENQANATP ATIFENKEKI
LKEDQTNASP ITSITSEKGE RSPFGDDQNN MPNVPNTTSE TDKSANFLKV EPQVLGSNSN
SANDGEIIEG LMQTHDVTLS NLRSRLTKLQ VVQHFWERND AKGAISALRK LPDQSVQADV
ISVLVDKMEI LTLDLFSCLL PVLTGLLDSN IERHVKVSLD MLLKLVAVFG PTIRSTISAP
PSVGIDLHAE QRRECSNQCF MQLQKIRMIL PILIRRGGIL AKSAQELNLV LQQP
//