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Database: UniProt
Entry: D8SX38_SELML
LinkDB: D8SX38_SELML
Original site: D8SX38_SELML 
ID   D8SX38_SELML            Unreviewed;       867 AA.
AC   D8SX38;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
DE   Flags: Fragment;
GN   ORFNames=SELMODRAFT_126954 {ECO:0000313|EMBL:EFJ11018.1};
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:EFJ11018.1, 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. Ungrouped subfamily.
CC       {ECO:0000256|ARBA:ARBA00010103}.
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DR   EMBL; GL377650; EFJ11018.1; -; Genomic_DNA.
DR   RefSeq; XP_002987944.1; XM_002987898.1.
DR   AlphaFoldDB; D8SX38; -.
DR   STRING; 88036.D8SX38; -.
DR   EnsemblPlants; EFJ11018; EFJ11018; SELMODRAFT_126954.
DR   Gramene; EFJ11018; EFJ11018; SELMODRAFT_126954.
DR   KEGG; smo:SELMODRAFT_126954; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   HOGENOM; CLU_014436_0_0_1; -.
DR   InParanoid; D8SX38; -.
DR   OMA; GFCEDIA; -.
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   CDD; cd00106; KISc; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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   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          8..354
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REPEAT          609..651
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          650..693
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REGION          557..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          370..502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        560..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93..100
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:EFJ11018.1"
SQ   SEQUENCE   867 AA;  95863 MW;  EF23E5C4A47A10C7 CRC64;
     GCGAVSGRVR VAVRIRPRNA EELIVDADFG DCVELQPELK RLRLRKNNWD CETYQFDEVF
     AETASQKRVY EVVAKPVVES VLEGYNGTVM AYGQTGTGKT FTLGRLGEED SADRGIMVRA
     MEDILSDISP ENDSVTVSYL QLYMETVQDL LAPERDNIPI VEDPKTGDVT LPGATLVPII
     DHRSFVRLLQ VGEANRFAAN TKLNTESSRS HAILLVNVRK VGRAKPDREV VVLSENGNCV
     QVAKGNRVPT IRKSKLVIVD LAGSERVYKS GSEGHTLEEA KSINLSLTAL GKCINALAEN
     SPHVPTRDSK LTRILRDSFG GTARTSLIIT IGPSPQHRGE TASTIMFGQR AMKVENMVKL
     KEEFDYKGLC RRLESELDKL IVENERQAKA IFDSEEELEK RLEEARHCVA EAENKLASHM
     QMEKAKHQKE LMELSQKHTQ EVAVLMQTLA LERAQKDNLE KDSSSNDSTL QPDEALQLKQ
     LLKKESRLRE QAEQELRILK SGNSAVASEV LVLMHEMKRL NAVSNNEIIL SLQTRLDEET
     RAREALEKEI QALKQQLQVN DEVDEPRKSP EKDAGSGADS PAALLRPQSA RSENGGGQRA
     TIARLFEQVG LQKILSLLES EDIDVRVHAV KVVANLAAEE ANQEKIVEAG GLHSLLSLLR
     GSEDETIRRV AAGAIANLAM NEINQELIMT QGGIGLLAKT SDEADDPQTL RMVAGAIANL
     CGNDKLQMRL REEGGIRALL GMVRSRHPDV LAQVARGIAN FAKCESRAAA QGYRNGRSLL
     IDDGALPWIV ANANNEASPI RRHIELALCH LAQHEVNAKD LVAGGALWEL IRISKECSRE
     DIRNLAFRTL NASPTYQAEL RRLHLAY
//
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