ID A0A453D3S0_AEGTS Unreviewed; 1222 AA.
AC A0A453D3S0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv21075600.9, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv21075600.9}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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 AlphaFoldDB; A0A453D3S0; -.
DR EnsemblPlants; AET2Gv21075600.9; AET2Gv21075600.9; AET2Gv21075600.
DR Gramene; AET2Gv21075600.9; AET2Gv21075600.9; AET2Gv21075600.
DR Proteomes; UP000015105; Chromosome 2D.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13200; FERM_C_KCBP; 1.
DR CDD; cd01366; KISc_C_terminal; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 6.10.250.760; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.25.40.530; MyTH4 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
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; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011254; Prismane-like_sf.
DR PANTHER; PTHR47972:SF16; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00784; MyTH4; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56821; Prismane protein-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS51016; MYTH4; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
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:UP000015105}.
FT DOMAIN 60..216
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 221..535
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 846..1167
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 542..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 682..794
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 542..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 927..934
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1222 AA; 139346 MW; 2828B021A240E403 CRC64;
MSIPPELAGA IPLIDRFQVE GFLKAMQKQI QSSGKRGFFI KKSVGPQVRE KFTLEDMLCF
QKDPIPTSLL KVPNDLVSRS IKLFHVILKY MGVDSPAIIS LEERIELVAK LYKHTLKRSE
LRDELFAQIS KQTRNNPDRS WLIRAWELMY LCASSMPPSK DIGAYLSEYV HYIAHGATTD
SDVRVLALNT LNALKRSVKA GPRVAIPARE EIEALLTSRK LTTIVFFLDE TFEEITYDMA
TTVADAVEEL AGIIKLSVYS SFSLFECRKI VNGSKSSEVG NEEYIGLDDN KYIGDLLSEF
KSAKDRNKGE ILHCKLVFKK RLFRESDEAV TDPMFVQLSY VQLQHDYILG NYPVGRDDAA
QLTALQILVE IGFIDNPESC VEWISLLERF LPRQVAITRA KRDWELDIIS RYQLMEHLSK
DDARNQFLRI LRTLPYGNSV FFSVRKIDDP IGLLPGRIIL GINKRGVHFF RPVPKEYLHS
AELRDIMQFG SSNTAVFFKM RVAGVLHIFQ FETKQGEEIC VALQTHINDV MLRRYSKARS
GSATSTVSQN DVSQADKPPN AEMYDKRVQE LSKVVDESQK KADQLRDELQ RKTQQEREMQ
EELEGLKDTL QSERHIIKEV TSERDRLKSL CDEKESSLQV ALVEKNRLET KLTNGQGQEN
NTKMDLSGNH CERDTLTTVG SVNSGIEMLT KLEEELKSCR KELAASKEVS KKLIMERNML
EQRIQRLERA KSEEKSTMQR VYEDECRKLK AHTATLEQKL ESATQSLNVA ESTLALRNTE
VDSLQNTLKE LDELREFKAD VDRKNQQTAE ILKRQGTQLV ELESLYKQEQ VLRKRYYNTI
EDMKGKIRVF CRLRPLNDKE VSLKDKNIVC SPDEFTIAHP WKDDKSKQHI YDRVFDAYTT
QEDVFEDTKY LVQSAVDGYN VCIFAYGQTG SGKTFTIYGS DNNPGLTPRA TSELFRVIKR
DGNKYSFSLK AYMVELYQDN LVDLLLPKNA MRQKLEIKKD SKGVVTVENV TVVNISSFEE
LKTIITRGSE RRHTAGTNMN DESSRSHLIL SIIIESTNLQ TQSYARGKLS FVDLAGSERV
KKSGSAGKQL KEAQSINKSL SALADVIGAL SSDGQHIPYR NHKLTMLMSD SLGGNAKTLM
FVNVSPAESN LEETHNSLMY ASRVRCIVND TSKHVSPKEI MRLKKLISYW KEQAGKRSEG
DELEEIQEER ISKEKADTRL TA
//
