ID A0A0C2YHC9_HEBCY Unreviewed; 964 AA.
AC A0A0C2YHC9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=M413DRAFT_59327 {ECO:0000313|EMBL:KIM49098.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM49098.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM49098.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN831768; KIM49098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2YHC9; -.
DR STRING; 686832.A0A0C2YHC9; -.
DR HOGENOM; CLU_001485_3_0_1; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000053424; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF32; KINESIN-LIKE PROTEIN; 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:UP000053424}.
FT DOMAIN 6..335
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 395..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 461..608
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 639..680
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 705..746
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 789..910
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 964 AA; 107456 MW; 6AE571B8928A4708 CRC64;
MASSTNIKVV CRFRPVNAIE QREGGDIVVA FDENLQTVQL KSNQVGSGPE KDGFTFDRVF
PMGTKQHEVF DYGVKDIVKD VLDGYNGTVF AYGQTGSGKT FTMMGADIDS DELKGIIPRI
TEQIFQSIVE SDAHLEYLVK VSYMEIYLER IRDLLAPQND NLQVHEEKSK GVYVKNLSDY
YVSSATEVYE IMRTGGAARV VSSTNMNAES SRSHSIFLIT IQQRNTETGA QKTGNLYLVD
LAGSEKVGKT GASGQTLEEA KKINKSLSAL GMVINALTDS KAKHIPYRDS KLTRILQESL
GGNSRTTLII NCSPSSYNES ETLSTLRFGI RAKSIKNTAR VNAELSPLEL KGLLQKAQLA
NTSYQKYIAL LEAELTRWRS GETVEEAEWA LPGKAAMAST ASMTKKPPTS PPPSTPASTS
RSMTPVNPSI EGLRSDLESR PQTPTVVGLD KDEREDFLRR ENELSDALAE KESTLSAAER
LVKELREELT YLKEQEASVS KENKAMSSQL NELRLQVERL DYDNKEGIIT VDILKEQNQD
AKAELEELKK QISDLKTAQK DASAGDKEKR KQEKMAMMMA KFDTQGAFSE KDEQLRQLLS
KLDNMDQDAP EVLSSEDLTA IRRQLSEGQT SARETVERLR QAHEENDMIT RRRDELEARV
TALEMEYEEL LAEKTIHEEE VNNVDVAELM ADLKNKLEIQ YATKRDALLS EVADLKQQLE
VRNNEVRSLN GSIDSLKSVN EELKRAFAVT SAGIEGGKNL AESAQDLERT RKAINVQLAE
FDGVKKSLMR DLQNRCEKVV VELEIQLDEM KEQYTNVIRN SNNKAQQKKM AFLERNLEQL
TLVQKQLVDQ NSTLKKEAGI AERKLLARNE RIQNLEALLQ DADRRLSIQN QKFETQLQAV
KERLDQARAQ KSVTSSTLNF GRIAKPLRGG GGASNISGPI AATSGGPSAS PLARLQNEEA
GCVK
//