ID A0A1B7NIJ1_9AGAM Unreviewed; 972 AA.
AC A0A1B7NIJ1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Kinesin heavy chain {ECO:0000313|EMBL:OAX44670.1};
GN ORFNames=K503DRAFT_764864 {ECO:0000313|EMBL:OAX44670.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX44670.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX44670.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX44670.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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; KV448123; OAX44670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7NIJ1; -.
DR STRING; 1314800.A0A1B7NIJ1; -.
DR InParanoid; A0A1B7NIJ1; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000092154; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; 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 CDD; cd01369; KISc_KHC_KIF5; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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; 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|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000092154}.
FT DOMAIN 6..335
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 386..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 464..561
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 636..670
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 708..742
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 788..905
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 402..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 972 AA; 108387 MW; 0F3113F4FDCD5133 CRC64;
MASSTNIKVV CRFRPPNSLE LREGGDIVVA FDENLQTVQM KNSQAVSGPE KDGFTFDRVF
PMGTKQHEVF DYGVKDIVKD VLDGYNGTVF AYGQTGSGKT FTMMGADIDS SELKGIIPRI
TEQIFKSIVE SDSHLEYVVK VSYLEIYLER IRDLLAPQND NLQVHEEKSR GVYVKNLSDY
YVSSAREVYE IMRQGGAARV VTSTNMNAES SRSHSIFLIT IQQRNTETGA QKSGNLYLVD
LAGSEKVGKT GASGQTLEEA KKINKSLSAL GMVINALTDS KVKHIPYRDS KLTRILQESL
GGNSRTTLII NCSPSQYNES ETLSTLRFGI RAKSIKNTAR VNAELSPLEL KGLLSKAQLA
NTRHLSYIQA LESELAIWRA GGHVEPSEWA TSDKPTTGAA AAAKKATSSP TPSTTRSMTP
VNPVLESLRS EMIDSRPQTP TVVSLDKDER EEFLRRENEL SDQLAERESV LAAAEKLAKE
LREELAYLKE QETSTSKENK SMSTQLNELR LQLERLDYDN KEGIITIDIL KEQNQDAKNE
LEELKKVITD LRSTQRDASA EDKEKRKQEK MALMMAKFDA QGTFSEKDEQ LRQLLAKLDT
IDSEVALSTL SVDDVVTARR QLAENHSLVR ETVDRLRQSQ EENEMITRRR DELEARFLAL
EADYEELLEK TIRDEETSNA DIVESMADFK NKLEVQYAAK RDANIGEVSD LKQQLELKTN
EIRTLNASID SLKSVNEELK RAFAVTSAGI EGGKNLAESA QDLERTRKAI NVQLAEFDGV
KKSLVRDLQN RCEKVVELEI QLDEIKEQYN NVIRNSNSKA QQKKMAFLER NLEQLTLVQK
QLVDQNSALK KEAGIAERKL LARNERIQNL EILLQDADRR LTIQNQKFEA QLQSVKERLD
QARAQKSSSA LGFGRIAKPL RGGGGSAAAV GTTTTPAPVS GGAPSASPLA RIQNEEGGGA
KRASWFFNPR GS
//
