ID A0A061DPK6_THECC Unreviewed; 1068 AA.
AC A0A061DPK6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Di-glucose binding protein with Kinesin motor domain isoform 1 {ECO:0000313|EMBL:EOX91893.1};
GN ORFNames=TCM_000957 {ECO:0000313|EMBL:EOX91893.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX91893.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX91893.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001879; EOX91893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DPK6; -.
DR STRING; 3641.A0A061DPK6; -.
DR EnsemblPlants; EOX91893; EOX91893; TCM_000957.
DR Gramene; EOX91893; EOX91893; TCM_000957.
DR eggNOG; KOG0239; Eukaryota.
DR InParanoid; A0A061DPK6; -.
DR OMA; DECYQSW; -.
DR Proteomes; UP000026915; Chromosome 1.
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; cd01366; KISc_C_terminal; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
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; IPR021720; Malectin_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972:SF18; KINESIN-LIKE PROTEIN KIN-14R; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF11721; Malectin; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000026915}.
FT DOMAIN 418..740
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 968..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..418
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 761..935
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 968..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501..508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1068 AA; 121025 MW; 0031F8916DE362BB CRC64;
MDDSQLNAFL QNPDTLFTNP SIPRVFDWEK NDMALNQDKP SSAMDEDEEE SSVDSMLCDS
NSRLIPFGFS KSNCTDEIMM FINAGGEALN EADSRMKFLG DSYFEGGNVM QTNEHIAEAG
DCPFIYQSAR FGSFCYRFNN FPPGDYFVDL HFAEIINTNG PKGMRVFNVY MQEEKVLSDF
DIFSVVGANK PLQVDDLRVS VKEDGLIAMR FEGVIGSPIV CGICVRKAQN IPVPQASQEY
LKCNNCAADI EVSSAQKKLM RTKVTDKYEK KIQELTTQCQ LKTHECHEAW MSLTAANEQL
EKVRMELDNK IFQTRTLDET VGKQAENLKN ITSRYGHDKK YWAAAVHDLQ EKIMIMKNEH
AQLSHDAHAC AESIPELNKM VTGIQALVAQ SEDLKLKYSE EQAKRKELYN QIQETKGNIR
VFCRCRPLSK EEISAGCALV VDFDAAKDGD LGILTGGSTK KTFKFDQVYT PKDNQVDVFA
DASPLVTSVL DGYNVCIFAY GQTGTGKTFT MEGTDQNRGV NYRTLEQLFQ IAKERSETFM
YNISVSVLEV YNEQIRDLLS TSPTSKRLEI KQSAEGFHHV PGIIEAKVDN IKEVWNVLQI
GSNSRAVGST NVNEHSSRSH CILHIMVKSK NLMTGDCTKS KLWLVDLAGS ERLAKTDAQG
ERLKEAQNIN KSLSALGDVI YALATKSSHI PYRNSKLTHL LQDSLGGDSK TLMFVQISPS
ERDLSETLSS LNFATRVRGI ELGPAKRQVD TSELQKMKTM LDKARQESRS KDESLRKLEE
SLQNLESKAK GRDQVYKTQQ EKIKELECQL ELKTSMQNQS EKQVSQLSDR LKGREEICTG
LQQKVKELET KLKERQQSES ASYQQKVNYF ENKLKEQVQE SEASSLALQL KIKELERKLK
EQEQNPESIL LRQKIKELED RLREQEQQLQ CALARDFGDV MRATPNEGKC RRDDEFMSEA
EPHILRSSNS ISRPLSQGYK QPRVSDSLHE TRRKRYSRSG ETENNMVMSA SLNDKRARKS
DPPKIARVVR TAKPVTGAAQ GPLTHKRINR DQVQAAKERD TKKKIWSR
//
