ID   BIMC_EMENI              Reviewed;        1184 AA.
AC   P17120; C8VHR3; Q5B7W7;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Kinesin-like protein bimC;
GN   Name=bimC; ORFNames=AN3363;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2138511; DOI=10.1016/0092-8674(90)90350-n;
RA   Enos A.P., Morris N.R.;
RT   "Mutation of a gene that encodes a kinesin-like protein blocks nuclear
RT   division in A. nidulans.";
RL   Cell 60:1019-1027(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Important role in mitotic dividing cells. Microtubule motor
CC       required for spindle body separation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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; M32075; AAA33298.1; -; mRNA.
DR   EMBL; AACD01000055; EAA63331.1; -; Genomic_DNA.
DR   EMBL; BN001306; CBF82860.1; -; Genomic_DNA.
DR   PIR; A34795; A34795.
DR   RefSeq; XP_660967.1; XM_655875.1.
DR   AlphaFoldDB; P17120; -.
DR   SMR; P17120; -.
DR   STRING; 162425.CADANIAP00009681; -.
DR   PRIDE; P17120; -.
DR   EnsemblFungi; CBF82860; CBF82860; ANIA_03363.
DR   EnsemblFungi; EAA63331; EAA63331; AN3363.2.
DR   GeneID; 2874347; -.
DR   KEGG; ani:AN3363.2; -.
DR   VEuPathDB; FungiDB:AN3363; -.
DR   eggNOG; KOG0243; Eukaryota.
DR   HOGENOM; CLU_001485_33_2_1; -.
DR   InParanoid; P17120; -.
DR   OMA; NGVYMTP; -.
DR   OrthoDB; 179272at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IDA:AspGD.
DR   GO; GO:0003777; F:microtubule motor activity; IDA:AspGD.
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; IMP:AspGD.
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:0051228; P:mitotic spindle disassembly; IMP:AspGD.
DR   GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR   DisProt; DP00636; -.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR025901; Kinesin-assoc_MT-bd_dom.
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   Pfam; PF13931; Microtub_bind; 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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1184
FT                   /note="Kinesin-like protein bimC"
FT                   /id="PRO_0000125364"
FT   DOMAIN          81..416
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          901..1184
FT                   /note="Globular"
FT                   /evidence="ECO:0000255"
FT   REGION          1041..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          489..900
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        9..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1060
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1105..1119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         167..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         1006
FT                   /note="Phosphothreonine; by CDC2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        9
FT                   /note="S -> Y (in Ref. 1; AAA33298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="P -> G (in Ref. 1; AAA33298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="I -> M (in Ref. 1; AAA33298)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1184 AA;  131576 MW;  245CC9BF152DEB36 CRC64;
     MAGPQRATSG LPTRRTTTRQ PTRRAGSAIP ERQTSTASPA VSTKTAAISR TRTLKSPGEP
     ASVLAKRKER DIEREINEDT SIHVVVRCRG RNEREVKENS GVVLQTEGVK GKTVELSMGP
     NAVSNKTYTF DKVFSAAADQ ITVYEDVVLP IVTEMLAGYN CTIFAYGQTG TGKTYTMSGD
     MTDTLGILSD NAGIIPRVLY SLFAKLADTE STVKCSFIEL YNEELRDLLS AEENPKLKIY
     DNEQKKGHMS TLVQGMEETY IDSATAGIKL LQQGSHKRQV AATKCNDLSS RSHTVFTITV
     NIKRTTESGE EYVCPGKLNL VDLAGSENIG RSGAENKRAT EAGLINKSLL TLGRVINALV
     DKSQHIPYRE SKLTRLLQDS LGGRTKTCII ATISPARSNL EETISTLDYA FRAKNIRNKP
     QINSTMPKMT LLREFTAEIE KLKAELIATR HRNGVYMSVE SYEEMKMENE SRRIISEEQR
     AKIESMESSL RHKVQELLTL TSKFNDLKKD NDDTLAALCS TNDVLQQTDI VLQNTRAQLE
     EEEMLRCAHE ETEHQLQDVG KGLISTLGQT VEDINSLQSK LDRKAELDAT NAELWRASST
     EVSDVTKRID QRVEAFQTRH AKLLETTSVK VNEFIATEIS NIERTRSDLS EYNRSLDAAC
     NNAKAETSSA HEDMNNVLEE IKDLREEVKS KVGEGLNGLS AAAARISEEV IGEFTQLHSQ
     LHTSFNNLGK DLKSIFETMA THLSEQKNEI NRLRAELQSS NRQNIETTHK ASAHLAQAIE
     EEHVAAEAER EILMSQIKAL VEESRQKQFA RLRAKIDGVR TEISASGDML EQATTQHDRQ
     IDEWVFKSEQ FAKDVNASKD EIRTKLQNDW EAFDQRNSTI RKATESVHKE TVRIVDVQVD
     DMGRQMEALD DFVAKARSQN GRYRDAHIAT LDTIATGVRD SYSSIEGRVE NLTGRMNQFQ
     QEATHHHATL EESIAPLSND VRKPLTDLSS SFQNRSLEEY VATGVTPKKR KYDYISVLPS
     TESHEVLKSR LRTTKEMEVL PFNSDDQLSG PSSSPGGSPS KGFVYNDVED EVGTHAPTVT
     NVNPSNTGLR EVDANVAARP LVYSTGEKST DQDGSPVVSP DSATEAEGMN GPPSKRRRSN
     SVVADTKLPN KMLARRMAGM MEGRENVPPP GISNGRRLRG RPSP