ID D8R2N8_SELML Unreviewed; 1056 AA.
AC D8R2N8;
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 motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_83012 {ECO:0000313|EMBL:EFJ34100.1};
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:EFJ34100.1, 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}.
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DR EMBL; GL377570; EFJ34100.1; -; Genomic_DNA.
DR RefSeq; XP_002965262.1; XM_002965216.1.
DR AlphaFoldDB; D8R2N8; -.
DR STRING; 88036.D8R2N8; -.
DR EnsemblPlants; EFJ34100; EFJ34100; SELMODRAFT_83012.
DR Gramene; EFJ34100; EFJ34100; SELMODRAFT_83012.
DR KEGG; smo:SELMODRAFT_83012; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_004957_0_0_1; -.
DR InParanoid; D8R2N8; -.
DR OMA; LCHENAK; -.
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; cd01374; KISc_CENP_E; 1.
DR CDD; cd16649; mRING-HC-C3HC5_CGRF1-like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF33; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
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:UP000001514};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 111..430
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1009..1044
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 635..662
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 697..738
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 810..837
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 880..928
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1056 AA; 117516 MW; 064B86F3F8AB6868 CRC64;
MASTSASSRR SSSPFRFRRP SSVNGRIPGF QPASPSSISS PSSTGRASLG GGGGGSHRSL
TPTRSRSSSQ ALMTPPSMKY SSFNGGSSPF TPSSSSSMFD RVEFINRAKE SISVTVRFRP
LSSREIQKGD EVAWYADGDT TVRSEYNLAT FYAFDRVFGP ATTTRGVYDI AAQHVVAAAM
QGVNGTVFAY GVTSSGKTHT MHGDQKSPGI IPLAVKDVFS IIQDTPGREF LLRVSYLEIY
NEVINDLLDP AGQNLRVRED AQGTYVEGIK EEVVLSPAHA LSLIAAGEEH RHVGSNNFNL
FSSRSHTIFT LTIESSCRGE DFSDDEITLS QLNLIDLAGS ESSKTETTGL RRKEGSYINK
SLLTLGTVIS KLSDGKASHI PYRDSKLTRL LQSSLSGHGR ISLICTITPA SSSTEETHNT
LKFAQRAKRV ELHAAPNRIL DEKSLIKKYQ KEITHLKQEL EQLRRGLFER PFVVSNHDDL
LTLRQQLEAG HLKMQSRLEE EEQAKAALMG RIQRLTKLIL VSTKNTIPLS LPEKSTQRRR
HSFGEEEKHE SMHAVPEEHT PSGSSVSFEP PVDFKSRRRK SFSRKPDELP PITGTTMADQ
MDLLREQMKM LAGEVALCSS SLKRLSEQAV TNPEDDQLHM QMRKLKEEID EKRRQMSIIE
KRIAGSAEAS STNASGFEMS QTISKLISQL HEKAFELEIK SADNRILQEQ LQSQTNEINE
LQETVVSLRQ ELQASLEKRY SQPKSRKLSR TLLDFSITLI CLLQAAELTK LKKDYTHLLE
VKDGLYLENQ NLNEEASYAK ELASAAAVEL KHLADEVTKL SLQNSKLNSE LAAAEASAYR
TGTATVSKAN ANKMGRNPGA DEDILLDDCE LLPKESSRNY QELEKKLEES RQREVSLESD
LANMWVLVAK LKKEKEEAEA GRKFSTENGH TDGNGELTIN EETEQWGTLK ELKVYLKDEK
QRVSEMERFI SQLKTRIQEE KERESSNDPA PAPASIDEIF DEDRGSHVCK ICFEAPTAAV
LLPCRHFCLC KPCAVACSEC PLCRSSITDR IITYTS
//
