ID A0A0N0DE64_FUSLA Unreviewed; 1184 AA.
AC A0A0N0DE64;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Kinesin family member 11 {ECO:0000313|EMBL:KPA40694.1};
GN ORFNames=FLAG1_06433 {ECO:0000313|EMBL:KPA40694.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA40694.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA40694.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA40694.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000256|ARBA:ARBA00034704}.
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:KPA40694.1}.
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DR EMBL; JXCE01000124; KPA40694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0DE64; -.
DR OrthoDB; 536293at2759; -.
DR Proteomes; UP000037904; Unassembled WGS sequence.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IEA:UniProt.
DR CDD; cd01364; KISc_BimC_Eg5; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR047149; KIF11-like.
DR InterPro; IPR047241; KIF11-like_kin_motor_dom.
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; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR PANTHER; PTHR47970:SF12; KINESIN-LIKE PROTEIN KIF11; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF58113; Apolipoprotein A-I; 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 Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000037904}.
FT DOMAIN 93..431
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 18..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..467
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 491..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 751..778
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 44..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1184 AA; 132013 MW; 53323AC6C03CD1AF CRC64;
MVLLPIVAFQ RTTRSEREQS RIGVATGTRA PSTRPGVRAG SRAPSTRYGS SIATRNGAAS
PTPSVASVAT VNTIGTKRKE RDFEVDASTE ETNIQVVVRC RGRNEREVRE NSNVVVTADS
VRGKVVELSM GSNALTNRSY NFDRVFSPAA DQYMVFDDTV KPILDEMLSG YNCTIFAYGQ
TGTGKTYTMS GDMTETMGML SDDAGIIPRV LQTLFTKLEL DNVESTIKCS FIELYNEELR
DLLASDEGTK LKIYDDTSRR GHASTIVQGM EEKHIKDAAE GVKVLQEGSL KRQVAATKCN
DLSSRSHTVF TITTYVRKPN EHGVEALVSA GKLNLVDLAG SENIQRSGAE NKRAAEAGLI
NKSLLTLGRV INALVDKGSH IPYRESKLTR LLQDSLGGRT KTCIIATISP AKSNLEETIS
TLEYAFRAKN IKNKPQMNPM IEKKTLLKDF TMEIERLKSE LIATRQRNGV YLSNETYEEM
TAQSESRRIV NEEQSAKLET LEKNLRNKVQ ELFSLQSTFL GLKKDHEGTR AQLDDTKEVL
DQTEIVLSAT RQSLSEETKI RKAHQKTEQK LTEVGGELID KLHKTVSDVG GLHAKNRRKS
DLQSINRNTW TTSQNQVADV TSMVERRIGE FQEEQQEHIA TVGQRMGSFV DEELRKLSTT
QAFLDEHLGT FSESKKELLE SKQKSKDDMD GVLEEIKVVR DTVKERMGES LQSISHSAER
IAADMMNEMT AFHGQLHNSY SALGKDFKSV FEELVKHITA QRAECDNLKR QLQSATNTIV
LQNATISSRI QDALTEERRL AVDDRQKLMS QISTLINTQA ETQESRIQAK ASEIQKTITS
TCTNLEQAVD TYGEGMSSWD LKEGEMLEEV KKSRDQLKTK LKDDWTAADD HSSSIQATAK
SVHAETVRAV DEQIKDLDVQ MEALDDFVTR ARTENSHHHE THNRSVEALS NTVEESFGNI
SAHFKSTFDR VKNLGEEMEV DLGDLQDGLE PLKDQLCQPL ANLREDVTGT ALQEYQPTGE
TPAKIQYHYP TDLPRTEDHD LIISSIDEVI TPTKNNESTD KDATIVFADL DSSPHKMMTS
PVRPATRMSM VSASEHMGMP SSLREVNPNV PGNLTTGSVN YNPRASITSM PPERTMPLFK
RPTRVTRSTK KVGSRDPIIS EGGENVLPTA LEESLSRRKS PRIN
//
