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Database: UniProt
Entry: A0A388KNU8_CHABU
LinkDB: A0A388KNU8_CHABU
Original site: A0A388KNU8_CHABU 
ID   A0A388KNU8_CHABU        Unreviewed;      1402 AA.
AC   A0A388KNU8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CBR_g9092 {ECO:0000313|EMBL:GBG71678.1};
OS   Chara braunii (Braun's stonewort).
OC   Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC   Chara.
OX   NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG71678.1, ECO:0000313|Proteomes:UP000265515};
RN   [1] {ECO:0000313|EMBL:GBG71678.1, ECO:0000313|Proteomes:UP000265515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S276 {ECO:0000313|EMBL:GBG71678.1,
RC   ECO:0000313|Proteomes:UP000265515};
RX   PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA   Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA   Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA   Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA   Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA   Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA   Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA   Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA   Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA   Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA   Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA   Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA   Rensing S.A.;
RT   "The Chara Genome: Secondary Complexity and Implications for Plant
RT   Terrestrialization.";
RL   Cell 174:448-464(2018).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBG71678.1}.
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DR   EMBL; BFEA01000151; GBG71678.1; -; Genomic_DNA.
DR   STRING; 69332.A0A388KNU8; -.
DR   EnsemblPlants; GBG71678; GBG71678; CBR_g9092.
DR   Gramene; GBG71678; GBG71678; CBR_g9092.
DR   OMA; DRHYLIR; -.
DR   Proteomes; UP000265515; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13200; FERM_C_KCBP; 1.
DR   CDD; cd01366; KISc_C_terminal; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.25.40.530; MyTH4 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR47972:SF16; KINESIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00139; MyTH4; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56821; Prismane protein-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS51016; MYTH4; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265515}.
FT   DOMAIN          266..421
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          426..740
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          1089..1402
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          787..863
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        60..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1170..1177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1402 AA;  155931 MW;  C55494B75673EE79 CRC64;
     MQVSDWWGGG DFDVLGRGGG GGGGGGVGGA GGTRPPSPSK LGARGAAPAG AGVSAAAPGS
     GAAESSSSAA AGVSSHQSAA AVPKRNLSVE LPEGGDNMSV AAASGKVSPD AGDGFEEGGI
     YTPNGGAPPA GDDSDSDITD ITPRMNGRGS LWTDGWKRGV RALGWRDGHH ERVRSRRNSF
     TGDVPLDEPV DDESSSTYKS NGDVSVSQPS TDYNIPGMDK YQIDVFLKAV QKQIQSNAKR
     GLLWRKSAPA TGAKEIKYAV EDMMSFQKDP IPTSLLKMNA DLTTKAVKLF HGVLKYTGVD
     GGDISESDQV ALVIKLYKHT LKRAELRDEL FAQLMKQTRN NPNGDWCAKT WELMYLCASA
     MPPGKDFAGY LSEYVHENAH NKLLDPKAKK MASSTWDALK RSVKAGARRM VPSPEEVEAL
     KEGRKLTTIA FFLDDTFEEL KYDMTTTVSE AVEELSSIIK LKHFQTFSLF EYRKVVSGSK
     SPEPLADEHI GLDDNKYIGD IVAEFKQIKE RTKGEVVQCK LLFKKRLFRE TDEAITEPMF
     IQLSYVQAQH DYLLGNYPVG RDDAAQLSAL QILAETGPVG SPETSMDWPI QVERSIPRQI
     AVTRAKKDWE ADVLQRFKSM VHLSKDDARQ QLLRILRSLP YGNSVFFTVR RIEDPIGLLP
     GRLVLGINKR GVHFFRPVPK EYLHSAELRD IMQFGSSSTA VFFKMRVAGV LHIFQFETKQ
     GEDICVALQT HINDVMLRRY SRTRAAQAAA VAAATQSGQT TEMAATVAAV AAAGGSQKLG
     ELYEKHIQEM SEVLENANKK IDRMNEDLRS RDDERKKLQE EIEELKDRLR SEEQSRVEIS
     QEKERLQKAL DEKEIALNLA LAAGETKAAS AETIPETSFP PQVAALQAEA ESSPTASPAR
     RPVSARSMPS RKEMPSEMKE QQQKIRSLEN QVRELKSELK AKTDELRQLD QASKKTLKDK
     QLLEQKLQRL EKSKAGESRS LEQKFNQERE EYRSRMLEME TKLRDRTKEH QEAQNKLTEL
     AADIESMQSD LKEIEDLREM KEDIDRKNAQ TAGIVKRQAE QINELETLYK EEQILRKRYF
     NMMEDMKGKI RVYARCRPLS EKEKGDKEKH VIAMPDEFTI EHPWKDDKPK QHQFDHVFDS
     TVSQEQVFED TKYLVQSAID GYNVCIFAYG QTGSGKTFTI YGGQDHPGLT PRAIKELFRC
     MKRDGNKFSF ALKVYMLELY QDTLQDLLLP KNAKRQKLDI KKDSKGMVVV ENATLISVEN
     AEELEATVTR GIDKRHVSGT QMNAESSRSH LILSVIIEST NLQTQALVKG KLSFVDLAGS
     ERVKKSGSAG EQLKEAQSIN KSLSALGDVI SALATEEPHI PYRNHKLTML MSDSLGGNAK
     TLMFVNISPA ESNLDETHSS LR
//
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