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Database: UniProt
Entry: A0A1P8AMI8_ARATH
LinkDB: A0A1P8AMI8_ARATH
Original site: A0A1P8AMI8_ARATH 
ID   A0A1P8AMI8_ARATH        Unreviewed;       753 AA.
AC   A0A1P8AMI8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=ARK2 {ECO:0000313|EMBL:ANM57838.1, ECO:0000313|TAIR:AT1G01950};
GN   Synonyms=armadillo repeat kinesin 2 {ECO:0000313|EMBL:ANM57838.1},
GN   AtKINUb {ECO:0000313|EMBL:ANM57838.1}, gene B
GN   {ECO:0000313|EMBL:ANM57838.1};
GN   OrderedLocusNames=At1g01950 {ECO:0000313|Araport:AT1G01950,
GN   ECO:0000313|EMBL:ANM57838.1};
GN   ORFNames=F22M8.8 {ECO:0000313|EMBL:ANM57838.1}, F22M8_8
GN   {ECO:0000313|EMBL:ANM57838.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM57838.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:ANM57838.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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; CP002684; ANM57838.1; -; Genomic_DNA.
DR   RefSeq; NP_001320318.1; NM_001331317.1.
DR   AlphaFoldDB; A0A1P8AMI8; -.
DR   SMR; A0A1P8AMI8; -.
DR   ProteomicsDB; 214091; -.
DR   EnsemblPlants; AT1G01950.4; AT1G01950.4; AT1G01950.
DR   GeneID; 839306; -.
DR   Gramene; AT1G01950.4; AT1G01950.4; AT1G01950.
DR   Araport; AT1G01950; -.
DR   TAIR; AT1G01950; ARK2.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; A0A1P8AMI8; baseline and differential.
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; 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:SF31; ARMADILLO REPEAT-CONTAINING 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   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
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   Proteomics identification {ECO:0007829|PeptideAtlas:A0A1P8AMI8,
KW   ECO:0007829|ProteomicsDB:A0A1P8AMI8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..261
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REPEAT          495..537
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          536..579
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REGION          389..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         4..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   753 AA;  83213 MW;  4F5676C815EC527D CRC64;
     MAYGQTGTGK TFTLGRLGDE DTAARGIMVR SMEDIIGGTS LDTDSISVSY LQLYMETIQD
     LLDPTNDNIA IVEDPRTGDV SLPGATHVEI RNQQNFLELL QLGETHRVAA NTKLNTESSR
     SHAILMVHVK RSVVENEFPV SNEMESSSHF VRPSKPLVRR SKLVLVDLAG SERVHKSGSE
     GHMLEEAKSI NLSLSALGKC INAIAENSPH VPLRDSKLTR LLRDSFGGTA RTSLIVTIGP
     SPRHRGETTS TILFGQRAMK VENMLKIKEE FDYKSLSKKL EVQLDKVIAE NERQLKAFDD
     DVERINRQAQ NRISEVEKNF AEALEKEKLK CQMEYMESVK KLEEKLISNQ RNHENGKRNG
     EVNGVVTASE FTRLKESLEN EMKLRKSAEE EVSKVKSQST LKTRSGEGED AGITRLQKLL
     EDEALQKKKL EEEVTILRSQ LVQLTFEADQ MRRCLDRGAP GNSYSGTDSL PSRHSQARES
     VNGQKAPFAT LCEQVGLQKI LQLLESDDAN IRIHAVKVVA NLAAEEANQE KIVEAGGLTS
     LLMLLRSYED ETVRRVAAGA IANLAMNEVS QQLIVDQGGI SLLSLTAADA EDPQTLRMVA
     GAIANLCGND KLQARLWSDG GIKALLGMVR CGHPDVLAQV ARGIANFAKC ESRATTQGVK
     SGRSLLIEDG ALPWIVQHAN DEAAPIRRHI ELALCHLAQH EVNAKEMISG GALWELVRIS
     KECSREDIRS LAHRTLSSSP VFRSEIRRLG IQF
//
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