ID W7HI87_9PEZI Unreviewed; 946 AA.
AC W7HI87;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=DRE_01468 {ECO:0000313|EMBL:EWC43581.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC43581.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC43581.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC43581.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; KI966457; EWC43581.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HI87; -.
DR HOGENOM; CLU_001485_21_1_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01370; KISc_KIP3_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT DOMAIN 7..378
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 730..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..438
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 833..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 946 AA; 103244 MW; F57DF7F030B0B930 CRC64;
MQANASSIQV TVRVRPFTIR EAAQITKIDD GPTFFGDGSL AATPKPSLTN KGIRRVIKVV
DDQFLIFDPP EENPIARFGQ KIIGPRGKQQ KDMRFGFDRV FDENASQGEV YEQTTKNLLD
SVLDGFNATV FAYGATGCGK THTISGTKQQ PGIIFLTMDE LFQRIDDLKS EKTIELSMSY
LEIYNETIRD LLIPGGSKLG LSLREDSNST ISVAGLSTHR PANVQEVMDM IVMGNENRTM
SPTEANATSS RSHAVLQVNV GQKNKTAGLS EDVFSATLSI IDLAGSERAS VTKNRGERLL
EGANINRSLL ALGNCINALC DPSKKNHIPY RDSKLTRLLK FSLGGNCKTV MIVCVSPSSH
HYDETHNTLK YADRAKKIKT KVSRNMINVN RHVSQYVKAI YDLQQEVADL KKRLGDSVKE
AMDKIKKQQQ SRDLAMKEGV RRIRASYDAT IDLRKRKAND RGGIRMMERR IAVIKAWLFA
FNAFFANGMM PSESLDKIRT QAEDGIKDLE EKKQWLVQRL ENEPWDRSIE TALKSATDSL
ARLDGGAKED DLEILHREAN LQKEKGERDI LETLFLDELE TTAIEVLTKA HFDTIAELER
IRQMEPEEAL AEAPMALFNL IQACTVATGQ VITPNGQISV PEYVASTPGR KRTSSAAYSI
SPVKKISFTA GTITGPISEE LIVPKSPARG TPKRKVHTPN KKAITFKKRV RWREDVVDVE
QSENSLVRKF KKQESELQQR RGGSPPPPLA PRSSLAGDAG LGGIGVSKAK RAGSSGIAAP
FSHAPMEVHV DSSDSELMPP PPVPPVRASS TTSAPPVRRS RMAIGFLSKD AAGEGGTNSS
TSTPDIGRAG TLEEQLAADP TTGVTAGSTI AANQSPLREA DNVGNLINRS TNRTSYPTRS
GGPIANTASP TSSAGGHRNG AARSDSQREG AAEEPCLAVL TGWNNN
//
