ID M5G5X4_DACPD Unreviewed; 961 AA.
AC M5G5X4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=DACRYDRAFT_113720 {ECO:0000313|EMBL:EJU05661.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU05661.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU05661.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU05661.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; JH795856; EJU05661.1; -; Genomic_DNA.
DR AlphaFoldDB; M5G5X4; -.
DR STRING; 1858805.M5G5X4; -.
DR HOGENOM; CLU_001485_3_0_1; -.
DR OMA; HIYAMEV; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
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; cd01369; KISc_KHC_KIF5; 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:SF29; 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; 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|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT DOMAIN 4..333
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..482
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 513..540
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 607..803
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 961 AA; 106934 MW; 68D00AA29B9F1278 CRC64;
MSNNIKVVCR FRPQNTIETR EGGEVVVSFD DSLATVGLRS TAGLSGPEKD GFTFDRVFPM
GTKQHEVFDY GVKGIVSDVI NGYNGTIFAY GQTGSGKTFT MMGANIDSDE LKGIIPRIAE
QIFTAIQEAP QNIEFLVKCS YMEIYLERIR DLLAPQNDNL QIHEEKNKGV YVKGLIEEYA
TGPEAIYELL RQGGLARMVA ATNMNAESSR SHSIFLIIIN QKNLDTGAQK SGSLYLVDLA
GSEKIGKTGA TGQTLEEAKK INKSLSALGM VINALTDGKS THVPYRDSKL TRILQESLGG
NSRTTLIINC SPSSYNEAET LSTLRFGMRA KAIKNKARVN AELSPAELKL LLKKAQTDNA
AFQKLIADLE AELGTWRSGG QVDPAFWVKG MGAPMKKAPT PSSTTPARPS TPINPMVEGL
RGELESRPET PTVIGLEKDE RDEFLRRENE LTDQLGERES QLSAAEKELV ELRAELAGLR
GDVPPPPKES QIPPHSSELI ELRLERDRIS FEKKELTIAL EDEKQKNSEL VAQVEDLNKA
ALQSRTRKTS LAEGKEKKKA ELMALMMSKL ESHVGISDKD DQLQSTLTKL AGIDSNEGVQ
ALTLDDIALV RRQLAEEHEA LRNAMEKLQE VQEENALLSK RRQDLERRNA QIEADMEDVF
AKYEAKEGHA DFAYAEVKAT LEAQFTAKLE SQQSEIEDLQ KQVETRTRDI RNLSSELDSS
KGVNEELKRA FEATSAGLAG GKDLAETARE LERTRKAIAA QLAEFDNTKK ALMRDVQDRC
EKVIELEVQL DEMREQYSNV IRNSNTKAQQ KKMAILERNL EQVSLIQRQL VDQNALLKRE
AGASERKLIT RNERIAGLEA QLRHAMREIE DRDRRYAEQF RNVYQATEHL RTAQPSARIA
KPLRGGGGAN PPANGPLARL QGEEASASRE FLSLSQVKSR IDWTNVASKQ RASWFFSASR
S
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