ID D8RDN2_SELML Unreviewed; 690 AA.
AC D8RDN2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
DE Flags: Fragment;
GN ORFNames=SELMODRAFT_783 {ECO:0000313|EMBL:EFJ29284.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ29284.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL377577; EFJ29284.1; -; Genomic_DNA.
DR RefSeq; XP_002969196.1; XM_002969150.1.
DR AlphaFoldDB; D8RDN2; -.
DR STRING; 88036.D8RDN2; -.
DR EnsemblPlants; EFJ29284; EFJ29284; SELMODRAFT_783.
DR Gramene; EFJ29284; EFJ29284; SELMODRAFT_783.
DR KEGG; smo:SELMODRAFT_783; -.
DR eggNOG; KOG4280; Eukaryota.
DR HOGENOM; CLU_001485_22_3_1; -.
DR InParanoid; D8RDN2; -.
DR OMA; NMRKHIE; -.
DR Proteomes; UP000001514; 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; 3.40.850.10; Kinesin motor domain; 1.
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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF29; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:UP000001514}.
FT DOMAIN 2..339
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 406..567
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFJ29284.1"
FT NON_TER 690
FT /evidence="ECO:0000313|EMBL:EFJ29284.1"
SQ SEQUENCE 690 AA; 78847 MW; AAAE1134F5D7C249 CRC64;
ERVQVVVRCR PMSHQEAMDG RQCCIVVDQQ EKTIEVSGDG RRGSSNDSNI KVFTFDRVYD
SKCTQNQLYQ EVAHPIVQSV MHGYNGTVLA YGQTASGKTY TMEGFDDSPE LRGIIPHAFE
EIFSHISQSQ SSDRFLVRAS YLEIYNEEIR DLLAPSTSPG ARLELKESPD AGVYVRNLTC
LTVHSLSDII RLLMVGKKNR SVGATLMNQD SSRSHSIFTI TVETSVEDPE TGLHIRVGKL
NLVDLAGSER MSKTGATGDR LKELTNINWS LTALGNVISA LVDGRSTHIP YRDSKLTRLL
QDSLGGNTRT VMVANIGPAD YNYEESVSTL RYANRAKSIK NKPRINEDPK DALLREFQAE
IIRFIGLICV LKLMNSENCV NRLKAQLSGD AVNDLTKEIC TLKNEKEMVE KNLRNLRQQA
GCLRAEKERS DEEKQKLTEQ LLKQLKDMQT HYESFAKEKE DRDFLTNKLR ALEDKVLHGS
NNDNEKLVEK AKQQEEELAL YQHHIQERQQ LDEERQRKIA ELEVKCSTME EELEMKTTKF
RKLMACYQQS KADLASLRTE LQDTIHEFHR ERTDLLLSLR SLEQQHQLKS LVIEKFIPSE
ELAKIMKRVE WDDETERWVF QSMVANFQSG MSPFIVDPAN KQPLQRPASA VGRSRPPGSR
YHSYMLALPR MDNVLKIGLD IPKHTLYDYE
//
