ID   KN7B_TOBAC              Reviewed;         955 AA.
AC   Q8S949;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Kinesin-like protein NACK2;
DE   AltName: Full=NPK1-activating kinesin 2;
GN   Name=NACK2;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC   STRAIN=cv. Bright Yellow 2;
RX   PubMed=11955449; DOI=10.1016/s0092-8674(02)00691-8;
RA   Nishihama R., Soyano T., Ishikawa M., Araki S., Tanaka H., Asada T.,
RA   Irie K., Ito M., Terada M., Banno H., Yamazaki Y., Machida Y.;
RT   "Expansion of the cell plate in plant cytokinesis requires a kinesin-like
RT   protein/MAPKKK complex.";
RL   Cell 109:87-99(2002).
CC   -!- FUNCTION: Probable plus end-directed motor protein that may function in
CC       the NACK-PQR (NPK1-NQK1/MEK1-NRK1) MAP kinase signaling pathway, which
CC       is essential for somatic cell cytokinesis, especially for the cell-
CC       plate formation and its expansion. May regulate the activity and the
CC       localization of NPK1, probably by association through the non-catalytic
CC       region of the kinase. {ECO:0000269|PubMed:11955449}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8S950}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8S950}. Cytoplasm, cytoskeleton, phragmoplast
CC       {ECO:0000250|UniProtKB:Q8S950}.
CC   -!- INDUCTION: During the M phase of the cell cycle (at protein level).
CC       {ECO:0000269|PubMed:11955449}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-7 subfamily. {ECO:0000305}.
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DR   EMBL; AB071436; BAB86284.1; -; mRNA.
DR   RefSeq; NP_001312129.1; NM_001325200.1.
DR   AlphaFoldDB; Q8S949; -.
DR   SMR; Q8S949; -.
DR   STRING; 4097.Q8S949; -.
DR   PRIDE; Q8S949; -.
DR   GeneID; 107775653; -.
DR   KEGG; nta:107775653; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0000919; P:cell plate assembly; IGI:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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; IPR021881; NACK_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF11995; DUF3490; 1.
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   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..955
FT                   /note="Kinesin-like protein NACK2"
FT                   /id="PRO_0000422319"
FT   DOMAIN          36..357
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   COILED          366..443
FT                   /evidence="ECO:0000255"
FT   COILED          566..604
FT                   /evidence="ECO:0000255"
FT   BINDING         120..127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   955 AA;  107229 MW;  47175C8CF3C20B99 CRC64;
     MVIGTPVTTP LSKIVRTPSR VPGSRRTTPS KIREEKILVT IRVRPLSPKE QAAYDLIAWD
     FPDEQTIVSK NLNHERHTGP YSFDYVFDPT CSTSKVYEQG ARDVALSALN GINATIFAYG
     QTSSGKTFTM RGITESAVND IYGRIKLTTE RDFVLKFSAL EIYNETVVDL LNRESVSLRL
     LDDPEKGVIV EKQVEEIVKD EEHLKTLIGT VEAHRQVGET ALNDKSSRSH QIIRLTIESS
     IRENSGCVKS FLATLNLVDL AGSERASQTS ADGTRLKEGS HINRSLLTVT NVIRKLSCSG
     GKRSGHIPYR DSKLTRILQA SLGGNSRTAI ICTLSPALSH LEQSRNTLCF ATSAKEVTTT
     AQVNMVVAEK QLLKHLQKEV SRLEAELRSP DPAASPCLRS LLIEKERKIQ KMEEEMNELK
     RQRDLAQSQL ELERRSKKEL KGSDHHGPSR QVVKCLSFTP EDEEVSGASL STNLGRKSLL
     ERQAAIRRST NSTNPSMLVH EIRKLEMRQR QLGDEANHAL QLLHKEFASH RIGSQGATET
     IAKLFSEIKE LQKISCIPEQ IEIKDKASLK EEIARLRSQE SNIASLEQKL ENVQRSIDEL
     VMHLPSCHES ADSRTAPSKK KRVLPFNLSN TSNIPNIIRS PCSPMSPSSC NIVEGEIENR
     APPECNNVGS AGDSFCSQLS TPVKSKDDNC TPGSRQSNSV NMKKMQTMFK KAAEDNIRSI
     KAYVTELKER VAKLQYQKQL LVCQVLELEA NEAASDEADI SDQSPLSWHL VFEDQRQQII
     MLWHLCHVSL VHRTQFYMLF KGDPSDQIYL EVELRRLTWL DEHLAGLGNA SPALLGDDAA
     GYVSSSIKAL KQEREYLAKR VSSKLNAEER EMLYVKWDIP PDGKQRRRLQ LVNKLWSDPL
     NMQNVRDSAE VVAKLVGFCE TGEHVSKEMF QLNFVSPSDK KTWIGWNLIS NLLHL