CIN8_ASHGO
ID CIN8_ASHGO Reviewed; 945 AA.
AC Q8J1G7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Kinesin-like protein CIN8;
GN Name=CIN8; OrderedLocusNames=ACR010C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Alberti-Segui C., Dietrich F.S., Philippsen P.;
RT "Identification of kinesin-related proteins in the filamentous fungus
RT Ashbya gossypii.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Required for assembly of the mitotic spindle. Interacts with
CC spindle microtubules to produce an outwardly directed force acting upon
CC the poles. Following spindle assembly, CIN8 and KIP1 apparently act to
CC oppose a force that draws separated poles back together. This force
CC seems to be mediated by KAR3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Note=Spindle microtubules that lie between the poles. {ECO:0000250}.
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; AF378568; AAN87133.1; -; Genomic_DNA.
DR EMBL; AE016816; AAS51237.1; -; Genomic_DNA.
DR RefSeq; NP_983413.1; NM_208766.1.
DR AlphaFoldDB; Q8J1G7; -.
DR SMR; Q8J1G7; -.
DR STRING; 33169.AAS51237; -.
DR PRIDE; Q8J1G7; -.
DR EnsemblFungi; AAS51237; AAS51237; AGOS_ACR010C.
DR GeneID; 4619538; -.
DR KEGG; ago:AGOS_ACR010C; -.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_001485_33_3_1; -.
DR InParanoid; Q8J1G7; -.
DR OMA; QMNSKTY; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0000235; C:astral microtubule; IEA:EnsemblFungi.
DR GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:EnsemblFungi.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000073; P:initial mitotic spindle pole body separation; IBA:GO_Central.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IEA:EnsemblFungi.
DR GO; GO:0007019; P:microtubule depolymerization; IEA:EnsemblFungi.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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:0033047; P:regulation of mitotic sister chromatid segregation; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..945
FT /note="Kinesin-like protein CIN8"
FT /id="PRO_0000125365"
FT DOMAIN 22..409
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 190..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..562
FT /evidence="ECO:0000255"
FT COILED 634..675
FT /evidence="ECO:0000255"
FT COMPBIAS 190..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 945 AA; 106848 MW; 4ECA339E65909854 CRC64;
MPDHEVQTRK SRMLDDAQEE LNITVAVRCR GRNEREIKAK SSVVVTVPDV TGSNEVSINT
TDEVGIAAKM NSRTYTVDKV FGPSADQSLI FKEIAEPLFD DFMKGYNCTV LVYGMTSTGK
TYTMTGDEKL YDGQLSDSAG IIPRIMFKLF DALEATDSDF LVKCSYIELY NEELKDLLDE
SHDSSKRLRI FDSSSMNHSS RASSQSNSPR EPEVAHNGFS RRRQRPPPVK ANRMSATKQQ
LSESGSGIYV QNVQEFHIIN AREGINVLQK GLKHRQVAST KMNDFSSRSH TIFTIMLYKN
CDGELFRVSK MNLVDLAGSE NISRSGAQNQ RAKEAGSINQ SLLTLGRVIN SLADKSIHIP
FRESKLTRLL QDSLGGNTKT ALIATISPAK INADETSSTL EYAAKAKNIK NRPQLGALMM
KDILVKNISS ELAKIKSDFL STKSKDGIYM SHEHYQEIVN DLENCQTEIQ ESKRQIESLT
SQNNLLLKDK KASQEVTELQ NSKIKKLQST IEYLYDKIER QHHNETELAT TIHKLKEALH
TMQGSLKSYE THELRLQNDI KEVLYQGITS YRESMNQHLE KVKVSMLDKN LSIKENINNI
TTIFDDTLKS VEANGSDMCD TLVKLIKETP SMYLKEFNET VSSLKSELSS YSNALTNKLT
EISEENNHLR EYLDQHLFKN STQEVLDLRM ESVYQKVKND SDQLLSKLVS MVGAHVEESR
TLMVNSMKDT VNEIIDNERS LFQPIRDRWI ASCDNINQCD ASHQNFEAKS TSGLDKLKEL
SDASLKSSED AVNKAKHRTD SFHDFVQKLC CDQSLKKQMH DISDKHRMLE DHFDDNVKYF
KESSKGFEDM DCSIKKIIHE MSPEVGDIKS VETLMERINA RTFSPVRPTG KTPSRQVLKN
AITSKASSRS MSPIKTLDTN VRIISPVKRG TIEFGAEGPP TKKVR
