InterPro kinesin motor domain signatures (IPR001752, IPR019821) correctly support ATP binding, microtubule binding and microtubule-based movement for Cut7.

Phylogenetic (kinesin-5/BimC family) inferences for plus-end-directed motor activity, mitotic spindle assembly, spindle pole body separation and spindle localization are consistent with the experimental data for Cut7.

The Swiss-Prot subcellular-location-derived spindle pole body annotation matches the directly observed SPB localization of Cut7.

Curator inferences of ATP hydrolysis activity and microtubule-associated complex membership follow from the demonstrated motor activity and the kinesin-5 tetrameric architecture.

ARBA electronic annotations (initial SPB separation, microtubule cytoskeleton) are consistent with the experimentally supported functions of Cut7.

Combined automated annotation of microtubule motor activity is consistent with direct experimental evidence for Cut7.

Cut7 concentrates on/near spindle pole bodies throughout mitotic and meiotic division and associates with spindle microtubules in a stage-specific manner including the anaphase B midzone; cut7 mutants form two unconnected half-spindles and fail chromosome separation.

Genome-wide YFP localization assigns Cut7 to the nucleus, microtubule cytoskeleton and mitotic spindle pole body, consistent with directed-evidence localizations.

The cut7-22(ts) allele is essential for spindle bipolarity; its bipolarity defects are rescued by stabilizing microtubules or deleting kinesin-14 pkl1, establishing the Cut7-Pkl1 force antagonism at the MTOC/spindle.

Discovery of cut7+; its product has a kinesin-heavy-chain-like N-terminal head domain and resembles A. nidulans bimC; cut7 mutations block spindle formation.

Acute inactivation of cut7 collapses the metaphase spindle into a monopolar structure; Cut7 is the active outward-force producer that slides interpolar microtubules apart and is indispensable for spindle length maintenance in fission yeast.

Mad1 binds Cut7 and recruits it to kinetochores of misaligned chromosomes to promote plus-end-directed chromosome gliding toward the spindle equator (chromosome congression), a context-specific role.

Full-length Cut7 is bidirectional in vitro; stepping direction is set by motor crowding on the microtubule lattice (greater crowding -> plus-end-directed). The N-terminus binds microtubules directly and increases occupancy.

Cut7 and kinesin-14 Pkl1 are antagonistic; co-deletion restores bipolarity. Cut7 also contributes to anaphase B spindle elongation (its loss reduces elongation velocity ~30%) in addition to bipolar spindle assembly.

Cryo-EM of the Cut7 motor domain on fission yeast microtubules shows canonical kinesin microtubule binding (helix-α4), a plus-end-docked neck linker, and slow microtubule-stimulated ATPase; loop5 divergence renders Cut7 resistant to the mammalian kinesin-5 inhibitor STLC.

Cut7 crosslinks antiparallel polar microtubules to drive spindle pole separation; its concentration is constant between mitosis and meiosis I, and it is required for meiotic (MI) bipolar spindle assembly, where kinesin-14 Klp2 antagonizes it.