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Database: UniProt
Entry: A0A061DI34_THECC
LinkDB: A0A061DI34_THECC
Original site: A0A061DI34_THECC 
ID   A0A061DI34_THECC        Unreviewed;       916 AA.
AC   A0A061DI34;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=TCM_000672 {ECO:0000313|EMBL:EOX91511.1};
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:EOX91511.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX91511.1, 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,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   EMBL; CM001879; EOX91511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061DI34; -.
DR   EnsemblPlants; EOX91511; EOX91511; TCM_000672.
DR   Gramene; EOX91511; EOX91511; TCM_000672.
DR   HOGENOM; CLU_001485_4_2_1; -.
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; cd01372; KISc_KIF4; 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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF3; KINESIN-LIKE PROTEIN KIN-4B; 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:UP000026915}.
FT   DOMAIN          8..365
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          696..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          373..431
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          494..628
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          851..892
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        704..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   916 AA;  103170 MW;  77BD9CA8191B5A23 CRC64;
     MEAAENCSVK VAVHIRPLIG DERTQGCKES VTVTSGKPQV QIGTHSFTFD HVYGNGGSPS
     SSMFEECVAP LVDGLFQGYN ATVLAYGQTG SGKTYTMGTA MKDGCQTGLI PQVMNALFKK
     IETLKHQTEF QLHVSFIEIL KEEVRDLLDS EPVSKSVTPN GNAVKVTVPG RPPIQIRESS
     NGVITLAGST EVAVTTLQEM ATCLEQGSIS RATGSTNMNN QSSRSHAIFT ITLEQMCKIQ
     SVSSGNDTLD NDMGEEYLCA KLHLVDLAGS ERAKRTGSDG LRLKEGIYIN RGLLALGNVI
     SALGDEKKRK EGVHVPYRDS KLTRLLQDSL GGNSKTVMIA CISPADINAE ESLNTLKYAN
     RARNIQNKPV VNRDLISNEM QKMRQQLQYL QAQLCARGGP TSDMQILKER ISWLEATNED
     LRRELHEYRS RRAVVECCES DAQEGHSCFM KSDGHKRGFQ SMDSSDYQMD EAVSDESPEE
     IDEVAKELEH ALRRNTMDRE LIELNKRLEQ KESEMKLVGG ADAEALKQHF RKKIMELEDE
     KRIVQIERDH LLVAVENRAA HSDGQVQKTQ EMNVQKLKAL EAQISDLKKK QENQVELLKQ
     KQRSDEAAKR LQAEIQYIKA QKVQLQHKIK QEAEQFRQWK ASREKELLQL RKEGRRNEYE
     RHKLEALNQR QKMVLQRKTE EAAMATKRLK ELLEARKSST RDNSVNHNGH APNGQSNEKS
     VRRWLDQELE VMVNVREVRF EYEKQTQVQT ALTEELTLLK QVDELSSNGD IPHIVNNGQS
     RLLSMSPNAR MERIASLEHM LSMSSNVLKA MASQLSEAEE RERGLVGRGR WNQVRSINDA
     KNLLQHLFNA TAEARCQLQE KDLEIKDLKQ QLKDLTALLW QSEAQKKELV KEQKMREQAV
     AIALATSASA AHPIGA
//
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