GenomeNet

Database: UniProt
Entry: F9GFC3_FUSOF
LinkDB: F9GFC3_FUSOF
Original site: F9GFC3_FUSOF 
ID   F9GFC3_FUSOF            Unreviewed;       519 AA.
AC   F9GFC3; A0A0D2XCN2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=FOXB_17357 {ECO:0000313|EMBL:EGU72113.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU72113.1};
RN   [1] {ECO:0000313|EMBL:EGU72113.1, ECO:0000313|Proteomes:UP000002489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU72113.1,
RC   ECO:0000313|Proteomes:UP000002489};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
RN   [2] {ECO:0000313|EnsemblFungi:FOXG_01655P0}
RP   IDENTIFICATION.
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936
RC   {ECO:0000313|EnsemblFungi:FOXG_01655P0};
RG   EnsemblFungi;
RL   Submitted (NOV-2023) to UniProtKB.
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; AFQF01006928; EGU72113.1; -; Genomic_DNA.
DR   STRING; 660025.F9GFC3; -.
DR   PaxDb; 5507-FOXG_01655P0; -.
DR   EnsemblFungi; FOXG_01655T0; FOXG_01655P0; FOXG_01655.
DR   Proteomes; UP000002489; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 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:UP000002489}.
FT   DOMAIN          1..335
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          440..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          372..431
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        455..476
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         80..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   519 AA;  58911 MW;  30AAEC508E7D92F2 CRC64;
     MDPITQLTTL SAPDDPDPEA AKLKAKKVIE EKKFTFDNSF WSHDTNDKHY ATQEDVYNSL
     GEDFLDHNFE GYHTCIFAYG QTGSGKSYTM MGTPDQPGLI PRTCEDLFER IDAAHCENSN
     VAYNVRVSYF EVYNEHVRDL LVPPQTHKAP NYLKIRESPT EGPYVKDLTE VPVRNINEIL
     RYMKLGDTSR TVASTKMNDT SSRSHAVFTI MLKQIHHDME TDETTERSSR IRLVDLAGSE
     RAKATEATGA RLREGSNINK SLTTLGRVIA ALADPKAGRG GKRKEVVPYR DSILTWLLKD
     SLGGNSKTAM IACIAPSDYD ETLSTLRYAD QAKRIRTRAV VNQDHISTAE RDAQIAAMAE
     EIRILQLSVS DSRQREKNAK EAEDKLEEYQ THVNSMQRMM EERSMVAESK IKKLQTENEA
     LKLHLKLAIE SLKNPIPPVV VKPEREVDEQ DKENASEYSE YDDDQYDSES TAYGEDELQE
     EMQQYLQDMG NLRKLMQGDL TRFKNENSAR MPLGAKETL
//
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