ID   D0A0B1_TRYB9            Unreviewed;       718 AA.
AC   D0A0B1;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=MORN repeat-containing protein 3 {ECO:0000256|ARBA:ARBA00039854};
GN   ORFNames=TbgDal_X17720 {ECO:0000313|EMBL:CBH16669.1};
OS   Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH16669.1, ECO:0000313|Proteomes:UP000002316};
RN   [1] {ECO:0000313|Proteomes:UP000002316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX   PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA   Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA   Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA   Barry J.D., Berriman M., Hertz-Fowler C.;
RT   "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT   chronic human african trypanosomiasis.";
RL   PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000256|ARBA:ARBA00004218}.
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; FN554973; CBH16669.1; -; Genomic_DNA.
DR   RefSeq; XP_011778933.1; XM_011780631.1.
DR   AlphaFoldDB; D0A0B1; -.
DR   GeneID; 23865012; -.
DR   KEGG; tbg:TbgDal_X17720; -.
DR   VEuPathDB; TriTrypDB:Tbg972.10.17720; -.
DR   OrthoDB; 5471784at2759; -.
DR   Proteomes; UP000002316; Chromosome 10.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
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   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46511; MORN REPEAT-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR46511:SF1; MORN REPEAT-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF02493; MORN; 6.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00698; MORN; 5.
DR   SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          9..260
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          678..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   718 AA;  81139 MW;  F4808794DFC0D503 CRC64;
     MENSSSFDRV RIAVRERPIA EEDILGVKLH VRQSEGKLFA YSPDATEGLM YDCDYFFPCS
     AKQEELYHAI GLEMIDLVAQ GLSSNVVVMG FAVTGKTHTL FGDNESVGLI YDTVGGLYQR
     LGAVAGEFET DIVLRYWEMN RDSVEDNLLD EDGSERAYTV TRDTFDRLVI PNLMAVRVPT
     FEDFLEQLER GNRNRVRRTK QRQSRWHGFL QLMVSTTPKV DSGKTVIRSM TFVHLKGTDC
     LGLKGVAGDQ LKEGCGINVS VTLLRAAVIH SINYREKRRS RATTPEGHHD LICSSQSFFM
     ECKFSRLMSQ FISGLEASFV VGCTNPLQFK ESIDTLENLQ YFRRLRCALK AIVVVSERGL
     LLKELRRQEE LLGAEAVAEL YGSDANGCPL NEAEEKLLQI YRKLHGFDPR RGAVKSPAVD
     PEAAIIERCK TRAQRLHGKV DTHGMRKRIF LTPRKTESYE GQWEDGKFGG FGELLKKLSK
     YRGEFRNGLR EGEGTLWLRK DVKSPWVRVY RGEWLAGKRD GVGISWEENG DVYEGGWSGG
     KRDGFGRLFF ANGDIYKGEF RDDQHYGRGI LRLTSGDWYD GYWALGLREG PGLWCYTQKQ
     QYFVGEWSKG ICKCGTMLDM PDKTTNENSR FIPRLGLLRC DEVLELEQLK LRDRRAQEYP
     EMNVEWRTPL VSAPLGALSK NVDSTSGGGD DLDAGNSSRD GEESVGTNVA EGWGLDVE
//