CUT7_SCHPO
ID CUT7_SCHPO Reviewed; 1085 AA.
AC P24339;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Kinesin-like protein cut7;
DE AltName: Full=Cell untimely torn protein 7;
GN Name=cut7; ORFNames=SPAC25G10.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2145514; DOI=10.1038/347563a0;
RA Hagan I., Yanagida M.;
RT "Novel potential mitotic motor protein encoded by the fission yeast cut7+
RT gene.";
RL Nature 347:563-566(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Could be a spindle pole body motor. On transition from G2 to
CC M phase of the cell cycle, the spindle pole body duplicates; the
CC daughter pole bodies seed microtubules which interdigitate to form a
CC short spindle that elongates to span the nucleus at metaphase.
CC Mutations at cut7 block spindle formation.
CC -!- INTERACTION:
CC P24339; P87169: mad1; NbExp=3; IntAct=EBI-16168992, EBI-16079828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; X57513; CAA40738.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA94636.1; -; Genomic_DNA.
DR PIR; S14032; S14032.
DR PIR; T38378; T38378.
DR RefSeq; NP_594527.1; NM_001019956.2.
DR PDB; 5M5I; EM; 9.30 A; C=64-432.
DR PDB; 5M5L; EM; 9.30 A; C=64-432.
DR PDB; 5M5M; EM; 9.30 A; C=64-432.
DR PDB; 5M5N; EM; 9.30 A; C=64-432.
DR PDB; 5M5O; EM; 9.30 A; C=64-432.
DR PDB; 5MLV; EM; 4.50 A; A/D/G/J/O/P=1-432.
DR PDB; 6S8M; EM; 4.50 A; K=1-432.
DR PDBsum; 5M5I; -.
DR PDBsum; 5M5L; -.
DR PDBsum; 5M5M; -.
DR PDBsum; 5M5N; -.
DR PDBsum; 5M5O; -.
DR PDBsum; 5MLV; -.
DR PDBsum; 6S8M; -.
DR AlphaFoldDB; P24339; -.
DR SMR; P24339; -.
DR BioGRID; 279182; 38.
DR DIP; DIP-61701N; -.
DR IntAct; P24339; 1.
DR STRING; 4896.SPAC25G10.07c.1; -.
DR iPTMnet; P24339; -.
DR MaxQB; P24339; -.
DR PaxDb; P24339; -.
DR PRIDE; P24339; -.
DR EnsemblFungi; SPAC25G10.07c.1; SPAC25G10.07c.1:pep; SPAC25G10.07c.
DR GeneID; 2542732; -.
DR KEGG; spo:SPAC25G10.07c; -.
DR PomBase; SPAC25G10.07c; cut7.
DR VEuPathDB; FungiDB:SPAC25G10.07c; -.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_001485_33_2_1; -.
DR InParanoid; P24339; -.
DR OMA; NGVYMTP; -.
DR PhylomeDB; P24339; -.
DR Reactome; R-SPO-983189; Kinesins.
DR PRO; PR:P24339; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:PomBase.
DR GO; GO:0005875; C:microtubule associated complex; IC:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR GO; GO:0003777; F:microtubule motor activity; IDA:PomBase.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; TAS:PomBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:CACAO.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000073; P:initial mitotic spindle pole body separation; EXP:PomBase.
DR GO; GO:0140013; P:meiotic nuclear division; IC:PomBase.
DR GO; GO:0099606; P:microtubule plus-end directed mitotic chromosome migration; IGI:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:PomBase.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 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 Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1085
FT /note="Kinesin-like protein cut7"
FT /id="PRO_0000125370"
FT DOMAIN 72..421
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 987..998
FT REPEAT 999..1010
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..604
FT /evidence="ECO:0000255"
FT COILED 715..740
FT /evidence="ECO:0000255"
FT COILED 897..955
FT /evidence="ECO:0000255"
FT COMPBIAS 1049..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1011
FT /note="Phosphothreonine; by CDC2"
FT /evidence="ECO:0000250"
FT CONFLICT 34..61
FT /note="SASNPRKRREPPTIDTGYPDRSDTNSPT -> LRAILGNDVSLLLLTL (in
FT Ref. 1; CAA40738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1085 AA; 122133 MW; 5669277875559D58 CRC64;
MAPRVAPGGS QQFLGKQGLK AKNPVSTPNS HFRSASNPRK RREPPTIDTG YPDRSDTNSP
TDHALHDENE TNINVVVRVR GRTDQEVRDN SSLAVSTSGA MGAELAIQSD PSSMLVTKTY
AFDKVFGPEA DQLMLFENSV APMLEQVLNG YNCTIFAYGQ TGTGKTYTMS GDLSDSDGIL
SEGAGLIPRA LYQLFSSLDN SNQEYAVKCS YYELYNEEIR DLLVSEELRK PARVFEDTSR
RGNVVITGIE ESYIKNAGDG LRLLREGSHR RQVAATKCND LSSRSHSIFT ITLHRKVSSG
MTDETNSLTI NNNSDDLLRA SKLHMVDLAG SENIGRSGAE NKRARETGMI NQSLLTLGRV
INALVEKAHH IPYRESKLTR LLQDSLGGKT KTSMIVTVSS TNTNLEETIS TLEYAARAKS
IRNKPQNNQL VFRKVLIKDL VLDIERLKND LNATRKKNGV YLAESTYKEL MDRVQNKDLL
CQEQARKLEV LDLNVKSSRE QLQYVSKSNQ EHKKEVEALQ LQLVNSSTEL ESVKSENEKL
KNELVLEIEK RKKYETNEAK ITTVATDLSQ YYRESKEYIA SLYEKLDRTE RNNKENENNF
WNLKFNLLTM LRSFHGSFTD ETNGYFTLLN DFNASMEELL NTHSNQLLIS MTKITEHFQS
LDEALQSARS SCAVPNSSLD LIVSELKDSK NSLLDALEHS LQDISMSSQK LGNGISSELI
ELQKDMKESY RQLVQELRSL YNLQHTHEES QKELMYGVRN DIDALVKTCT TSLNDADIIL
SDYISDQKSK FESKQQDLIA NIGKIVSNFL QEQNESLYTK ADILHSHLND TNSNIRKANE
IMNNRSEEFL RNAASQAEIV GANKERIQKT VENGSQLLDS KSKAIHSNSR SMYDHCLALA
ESQKQGVNLE VQTLDRLLQK VKEHSEDNTK EKHQQLLDLL ESLVGNNDNL IDSIKTPHTE
LQKITDHVLK GTTSLANHTN ELLGLGDESL CNLETTIEDT SLVKLETTGD TPSKRELPAT
PSWTRDSSLI KETTNLNLDS DKKFVRETYT SSNQTNEPDV YDKPSNSSRT SLLRSSRSAY
SKMKR
