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Database: UniProt
Entry: F6HND6_VITVI
LinkDB: F6HND6_VITVI
Original site: F6HND6_VITVI 
ID   F6HND6_VITVI            Unreviewed;       989 AA.
AC   F6HND6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   OrderedLocusNames=VIT_13s0019g04750 {ECO:0000313|EMBL:CCB56155.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB56155.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Ungrouped subfamily.
CC       {ECO:0000256|ARBA:ARBA00010103}.
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DR   EMBL; FN595998; CCB56155.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6HND6; -.
DR   STRING; 29760.F6HND6; -.
DR   PaxDb; 29760-VIT_13s0019g04750-t01; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   HOGENOM; CLU_014436_0_0_1; -.
DR   InParanoid; F6HND6; -.
DR   Proteomes; UP000009183; Chromosome 13.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   CDD; cd00106; KISc; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR047149; KIF11-like.
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   PANTHER; PTHR47970:SF6; KINESIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR   Pfam; PF00514; Arm; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00185; ARM; 4.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 2.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..989
FT                   /note="Kinesin-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003337844"
FT   DOMAIN          29..374
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REPEAT          735..777
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          776..819
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   COILED          383..467
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          531..597
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          631..679
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         114..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   989 AA;  110599 MW;  613E803F2267BA2B CRC64;
     MGFKCLVFLL LSSMGGTYVE GELKADSGRV RVAVRLRPRN ADDLLSDADF ADCVELQPEM
     RRLKLRKNNW SSESYRFDEV FTESASQRRV YEVVAKPVVE SVLNGYNGTV MAYGQTGTGK
     TYTLGRLGND DASERGIMVR ALEDIIANTS PTSDSVEISY VQLYMESIQD LLAPEKINIP
     ITEDPRTGEV SLPGAAVVKI RDIDHFLQQL QIGEANRHAA NTKLNTESSR SHAILMVYVR
     RSVHKKVEDE ISSQEKVNRS DVPGGSRIPI VRKSKLLIVD LAGSERVDKS GSEGQLLEEA
     KFINLSLTSL GKCINALAEN SPHIPIRDSK LTRLLRDSFG GSARTSLIIT IGPSARHHAE
     TTSTIMFGQR AMKIVNMVKL KEEFDYESLC RKLEKQVDQL TEEIERQQKL RKNDTDELEK
     RLIECQNTFA EAEKNLVTRS EFLEKENTRL ELEMKDFLNE LNHQKDLNVL MRDEVASLEM
     SLKHSKQYQL ENSTCQQVLA DTTQMYEKKI AELIKQLGDE RARYETAGEQ LDVIKKLLSE
     SQQKIQQQKT ENSTYQKALA DTTQMYEKKI AELTKQLEDE HARFEGAEKQ LDEAKNLLSC
     HQKPMQQDEI DELKMRLHEM GRHQELSVNE LQSLQSEYND LLSEKATLTE ELHAVNQTLS
     VEEKQRKTIE NELVKLKKLV LENDHDFEDK KSYVKESIGK ESSAFGAPVG LHKSNPSRET
     ISGQRATIAK ICEEGKIFLI LALLTSEDLD VQIHAVKVVA NLAAEDINQE KIVEEGGLDA
     LLLLLRSSKS TTILRVASGA IANLAMNELN QGLIISKGGG QLLANMASKT DDPQTLRMVA
     GAIANLCGNE KLHMMLKEEG GIKALLGMVR SGNSDVIAQV ARGVANFAKC ESRGIIQGHR
     KGRSLLVEDG ALTWLISNCN TASASTRRHM ELALCHLAQN ENNAQDFKSS GGVRELKRIA
     AESTREDIQN LAKKTLKSTP FQAEIHAEL
//
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