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Database: UniProt
Entry: A0A443PV04_9MAGN
LinkDB: A0A443PV04_9MAGN
Original site: A0A443PV04_9MAGN 
ID   A0A443PV04_9MAGN        Unreviewed;      1028 AA.
AC   A0A443PV04;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Kinesin-like protein KIN-14G {ECO:0000313|EMBL:RWR94611.1};
GN   ORFNames=CKAN_02391300 {ECO:0000313|EMBL:RWR94611.1};
OS   Cinnamomum micranthum f. kanehirae.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX   NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR94611.1, ECO:0000313|Proteomes:UP000283530};
RN   [1] {ECO:0000313|EMBL:RWR94611.1, ECO:0000313|Proteomes:UP000283530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:RWR94611.1};
RX   PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA   Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA   Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA   Leebens-Mack J.H., Tsai I.J.;
RT   "Stout camphor tree genome fills gaps in understanding of flowering plant
RT   genome evolution.";
RL   Nat. Plants 5:63-73(2019).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-14 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010899}.
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:RWR94611.1}.
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DR   EMBL; QPKB01000011; RWR94611.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443PV04; -.
DR   STRING; 337451.A0A443PV04; -.
DR   Proteomes; UP000283530; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; 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:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd21203; CH_AtKIN14-like; 1.
DR   CDD; cd01366; KISc_C_terminal; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47972:SF39; KINESIN-LIKE PROTEIN KIN-14I; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
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   Plastid {ECO:0000256|ARBA:ARBA00022528};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283530}.
FT   DOMAIN          41..163
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          407..727
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          832..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          973..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          255..282
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        982..1009
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         490..497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1028 AA;  114422 MW;  E9E5C7588F4932AA CRC64;
     MAPEAAIFSI SMASVVEDVL QQHRTRLSDS DLASRKAEET AWRRYEAAGW LRKMIGVVGA
     KDLPAEPSEE EFRLGLRNGI VLCNVLNKIH PGAVTKVVEA PVDSVHLPDG AALSAFQYFE
     NVRNFLVAVQ EMGLPTFEAS DLEQGGKGAR VVNCVLALKS YSEWKQMGGN GSWRYGGNLK
     PTSLGKCFVR KNPEPFMSRN LSMNEKCLDG LSIEQNMNGD LYHESSEMTS SHSLNTLIRA
     VLSDKKPEEV PTLVESVLSK IMEELERRLA TQNEKVNTAL KDLSTSDGNK FLPKTKGSND
     VGMVMEHDDN WVKSNPNSCL KPFNDESRRQ LLKQQMLFDQ QQRDIQELKH TLQTTKAGMQ
     FIQMKYSEEL CNLGRHLHSL AYAASGYHRV LEENRKLYNQ VQDLRGNIRV YCRVRPFLPG
     QPNRISTLDC LDDGSITIIT PSKYGKEGRR SFNFNKVFGP SASQEEVFSD TRPLIRSVLD
     GYNVCIFAYG QTGSGKTYTM TGPKDLTEQS QGVNYRALRD LFNLSAQRRD TFCYDVAIQM
     IEIYNEQVRD LLVADEIRNN SQNGVNVPDA SLVPVASTSD VIELMNIGQR NRAVGATALN
     DRSSRSHSCL TVHVHGRDMT SGTILRGCMH LVDLAGSERV DKSEVTGDRM KEAQHINKSL
     SALGDVIAAL AQKNSHVPYR NSKLTQLLQD SLGGQAKTLM FVHVSPEVNA VGETISTLKF
     AERVATVELG AARLNKESGD VRDVKAQLAT LKAALERKEV EPDHYQNTVL SPEVHRMKAG
     GPSSIHSDQQ GGDVLVGQSN HRKPMQYVGN TEVRSDSAMR PKRPSFDLQE LLLSSNSPPW
     PDSSPRIDFQ KGDEQESSSG DWVDKLVVNK QEVITEGDNP FRRWNGNSGP LPEIFCPGYR
     PDMGIYSDQQ YDTQESRKDS HEYETEITDD SDELEIATSD SSEADMLWQF NLPKVAKPAS
     GFESRIKKPQ ITLVKSPDIR NAGQAHSPSH SQKISYGSLH LNRPGRQPVS NNRDGKRVLS
     GRKTGNGK
//
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