ID X0CR91_FUSOX Unreviewed; 869 AA.
AC X0CR91;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=FOQG_10971 {ECO:0000313|EMBL:EXK85027.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK85027.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK85027.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK85027.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; JH658392; EXK85027.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CR91; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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; PTHR24115:SF372; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 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|RuleBase:RU000394};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT DOMAIN 1..223
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 515..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 95153 MW; D91043A38C9E8EC6 CRC64;
MTMQELFEKI EERSQDKVTD LSLSYLEIYN ETIRDLLVPG GSRGGLMLRE DSNQAVTVSG
LTSHHPKDVQ EVMDMIVQGN EYRTVSPTEA NATSSRSHAV LQINIAQKDR SAGASEPHTM
ATLSIIDLAG SERASVTKNR GERLTEGANI NKSLLALGSC INALCDRRQK QHVPYRNSKL
TRLLKFSLGG NCKTVMIVCV SPSSAHFDET QNTLRYANRA KNIQTKVTRN VFNVNRHVKD
FLVKIDEQMA LINELKAQQK DAEAMFFAKF RKQCDKRDAM AREGIQRLRI AYENSASERQ
ERITNMKRLK AFERRIGMLS GWIAAFDTVC DERGDEDAMP ENLVAIRKTA QGILVELENS
RHHIHQKLEK SAWDRAIDTA LSHSLQQLQG TEGADNGEAD NLTREAELIK ANFNREAYRE
VLEQDKAGDA AMIQMLLTAQ FDILASLSDT LGMDEEEAVA HAKEMINRLL QTGFTAAGQV
VKPDGSMPVV EVFSPSKRGT PKRKKAIAMH IKPVSAPNFT PAHSDHAPVS PMKGSPRRRK
VLGASKKGVS FTPVKAKKKG GVRWRDDETE EGTLEDFSKT PQKYNSSPAI PSPEKPIVAP
IIPSYLEPET STVEESSPSL EIPEASSLGA KPSRFQAGFL SKGPRHSLAD GSPKAPTMTL
KLEASPDIQR TPPLRSLDVT KSGNFSPSPS GLGIPRAIRR LPTIHDENNP PGSGSDSETS
TIDARKLQTA LRTAMKEKAR RASIMAGTTA SSTKRVSSMG SLPERTGPRP SLPAALASSA
NGISRLRRGS AERRRSPPMA CSPNDFKIDM ALTPGQARRM NMNNTVTRME GPGSSPQGGM
AGSAPRRITI GTGGGAAHRR QDSRGYTLR
//
