ID A0A314KXV9_NICAT Unreviewed; 1069 AA.
AC A0A314KXV9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Kinesin-4 {ECO:0000313|EMBL:OIT34062.1};
GN Name=ATK4_2 {ECO:0000313|EMBL:OIT34062.1};
GN ORFNames=A4A49_04626 {ECO:0000313|EMBL:OIT34062.1};
OS Nicotiana attenuata (Coyote 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=49451 {ECO:0000313|EMBL:OIT34062.1, ECO:0000313|Proteomes:UP000187609};
RN [1] {ECO:0000313|EMBL:OIT34062.1, ECO:0000313|Proteomes:UP000187609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC TISSUE=Leaves {ECO:0000313|EMBL:OIT34062.1};
RA Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OIT34062.1}.
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DR EMBL; MJEQ01000778; OIT34062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A314KXV9; -.
DR STRING; 49451.A0A314KXV9; -.
DR EnsemblPlants; OIT34062; OIT34062; A4A49_04626.
DR Gramene; OIT34062; OIT34062; A4A49_04626.
DR Proteomes; UP000187609; Unassembled WGS sequence.
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 Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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 InterPro; IPR031852; Vik1/Cik1_MT-bd.
DR PANTHER; PTHR47972:SF4; KINESIN-LIKE PROTEIN KIN-14L; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16796; Microtub_bd; 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 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:UP000187609}.
FT DOMAIN 23..147
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 381..649
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 668..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 319..350
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 714..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 463..470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1069 AA; 118194 MW; F353F33424269623 CRC64;
MEDSRRGRGH EYNLAWRKAE EADLRRYQAT HWLECFVGPL GISSQPSEKE FVSCLRNGLV
LCNLINKVQP GSVPKVVENH TASHSIMWDS QPLPAYQFFE NIRNFLVAVE DLKLPAFEAS
VFERDNIEAG SLTKVVDCIL ELKAYHEWKQ MTGGVGCYKP LRSPLLTPSR GRIQTRQPMT
INSDSCRRLE MSAACPKQSA AEDEIQKIEG IIVKALAERL VDMKENMGNN FFASFRNGNV
NQVELFSRIL SSCFEEQPRN KLPKLKADPL KELNCSEDNS TCIPLQNLSN LRNRECCRAC
IKKGTCNHWT LVTMQEKELS NLKVLLSSTK REFEDLQSQL QSDLKQLGDQ VLEMSNAALG
YHKVLKENTT LHNMVQDLKG NIRVYCRIRP AFSAEAKTAI DFIGEDGSLV VIDPLKSWKD
GRKIFQFNRV FGPTATQEDV FRDTKPLVRS VMDGYNVCIF AYGQTGSGKT YTMSGPGEIR
TCMGGNGLPL PDASMHPVNC AADVINLMKL GDLNRAVGST AMNNRSSRSH SVLTVHVHGE
DTSGNIIHSC LHLVDLAGSE RVDKSEVTGD GLKEAQHINK SLSCLGDVIT ALAQKNSHIP
YRNSKLTLLL QNSLGGHAKT LMFAHVSPEG DSFGETVSTL KFAQRVSSVE LGAARLNKES
TEVLELKAEE TQTPQINKPK EAARTPFQKP KAIAERPTPR ARRLSIENCT TMRVEKANAD
DETGSKTPAA KTRSRRLSLE GPRLASKNLE RIKSLETTSK QDDKPEVVCL QKSSELQEGD
DITKLYDQVG NGSCMEAPHS PTSAFKRQQP PRSPTAGFKI QQAPRSPTSA YKRQQPPRSP
ISGFKSQQAP RSPTSFKSQL PPRSPTSGFK SKQAPRSPTS AYKSQQPPWS PTSVFKSCNA
PRSPTSAAIK SQGVKTTDNR TRIPSLQLPK TPEPLITSID EIKGGMRSER TISSEFQTPT
LISSTHGKGS QIRRSLRTIG KLINGSDRKN QQKRTEAAPL SPFNCQNEVK SPIASNARTL
RRQSLTGIPP PTMSRRSSLG GGTLPDSCAN ESRNSKTPPS RASSKSRWL
//
