ID A0A061HDG6_9BASI Unreviewed; 978 AA.
AC A0A061HDG6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=PFL1_03969 {ECO:0000313|EMBL:EPQ28666.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ28666.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ28666.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ28666.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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; KE361634; EPQ28666.1; -; Genomic_DNA.
DR RefSeq; XP_007879683.1; XM_007881492.1.
DR AlphaFoldDB; A0A061HDG6; -.
DR GeneID; 19318076; -.
DR KEGG; pfp:PFL1_03969; -.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_001485_3_0_1; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000053664; 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: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; 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:UP000053664}.
FT DOMAIN 4..333
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 535..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 630..671
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 822..909
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 959..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 978 AA; 107839 MW; A4D969AF9FDE5A8B CRC64;
MSSNIKVVSR FRPPNALELR EGGDIVVDFS DDGTLVKMTK GAGTSGPEAN GFVFDRVFPM
GTQQRDVFEF GIKETVDDVL NGYNGTIFAY GQTGSGKTFT MMGSDIDNDE LKGIIPRITE
QIFENIMASP PHLEYLVKVS YMEIYMEKIR DLLAPQNDNL QVHEEKNKGV YVKGLSDYYV
GGQADVYEIM RQGGSARVVS STNMNAESSR SHSIFLISIQ QRNTETGSQK TGNLYLVDLA
GSEKVGKTGA SGQTLEEAKK INKSLSALGM VINSLTDGKS SHIPYRDSKL TRILQESLGG
NSRTTLIINC SPCIFNAEET LSTLRFGVRA KSIKNKARVN AELSPAELKA LLKKAKADAD
RSQQYIANLE AELKVWRSGG KVPEPEWADA SKVIVGEGAS LAPAASQVAQ NGASRPMTPA
VEGLREISSR PDTPSAVTLD KDERDEFLRR ENELNDQIAE KEVLLQDVQK QHREASLELA
ACKESEAALS AENKSLTSKL TETELQLGKV NFQLKEVTIT IDSLKESNHD LSQEIEELKK
STSEGKGGAA KDPSQEGKER KKAEKMAKMM ADFNAGIVSE KEEQIRETLS KLENAGSLGG
AGAGGEGAVG LSADDLSTLR EQLLESQTLV REQQGRVRRA QEENELLLKR RDEVEMRLAA
LEAEYDELLE KTFKDEESSH VDHHHLDETI QDVKAKLEAQ YASKREAQAS EIADLKLQIE
LKGKETAELL ATNDNLKSTN EELKRAFAVT AAGVEGGKNL AESAREMERV RKTMATQLAE
FDIMKKSLMR DLQNRCEKVV ELEISLDESK EQYNNVLRSS NSKAQQKKMA FLERNLEQLT
NVQKQLVEQN SSLKKEVAIA ERKLSARNER IQALEHHLME SQEKLALQNR KFDEQLQAVK
ERLNQAREMR PNMMAGGGGA LSFGRIAKPL RGGGPTTGPQ PGPVAARHPG IVGAHQADTN
SPKARSSWFF SSKSKMDS
//
