ID A0A2S6CAT6_9PEZI Unreviewed; 1074 AA.
AC A0A2S6CAT6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=CBER1_11055 {ECO:0000313|EMBL:PPJ56840.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ56840.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPJ56840.1}.
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DR EMBL; PNEN01000507; PPJ56840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CAT6; -.
DR STRING; 357750.A0A2S6CAT6; -.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000237631; Unassembled WGS sequence.
DR GO; GO:0005819; C:spindle; IEA:UniProt.
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 GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01370; KISc_KIP3_like; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; 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 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:UP000237631}.
FT DOMAIN 12..384
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 654..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..433
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 655..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1074 AA; 116079 MW; DA1F638D1634BB79 CRC64;
MAAALPVDGA SSISVAVRVR PFTIQEAAQL TRNDDGPLFL GDGSMAAVPK PRVGGKGIRP
VIKVMDEKCL VFDPPEEHSV QRFGRAMLPQ GKRSKDQTFA FDRVFDEHTT QCDVYAATTQ
PLLDQVLDGY NATVFAYGAT GCGKTHTITG TVQSPGIIFM TMQELFERVQ ELRETKEVDV
TLSYLEIYNE TIRDLLAPPG SSGKQGLMLR EDSHQAVSVA GLTSNKPQSV EEVMDMVIQG
NGQRTQSPTE ANATSSRSHA VLQVNVALKD RNAAVNEPVT FATLSIIDLA GSERASVTKN
KGERLLEGAN INKSLLALGS CINALCDARK KNHVPYRNSK LTRLLKFSLG GNCRTVMIVC
VSPSSAHFDE TQNTLRYANR AKNIQTKSVR NVYNVDRHVK DYLKKIDEQM LLIKELQAQL
QDYEKQAFAK FKKAESKFDA VLKDSIERVR LAYDHSASER KERINTTLRL RQTERRIGAI
SGWVGAFDQV CETREEEEPA VAMIAMRKTA IGILAELEHS RQHHHQKLGK INWTRAIDIA
LQDGLRQLES NESFTADCAG ASSLLKEVEL LNHRADIEMN AIVLDAEKTG ESGLMNVMLT
THFETIAIVN QLAQMTEQEA VQAGREILGK LLQACTDAVG QVIKPDGGLQ ITAAVAPSRS
GTSRKQKSLI GPSPMKSKIR HSVSSRASLS SQPQPVLPAP AASAIPAHIA AEMSSVPPHE
GSSPARGTSA SPRRHVKKLG GLARKGVAFG SGTPRKRSPQ KKRGVRWRDE GAEDGSTPGA
LVEFQPTPKM PAPTPPSFNN DDSVTIEPPR FTSEIDANDA DPESSPLPLP PTQSSEIRKT
PAGTGRFAIG ALTKGSKLGS DSPTLMPPPK FSTSMGSFSS DDESSPLREL GNRAPHSSSL
RTVNNTSDQS DASFSTGGSD AEQSFTDREA SQQIRAAMAK KRRSSMGTRN SIGGGASRQR
ASDRAQRRRS PTAAQFAVGS PPSDSSFSAS HARRIGASRE STGHSNILSP RTGSVVKNNG
PPAVRAAQPL RVRQSMIDIN HTPRETPTGP NGRPHSRVSS VVPGSAGGSK PVWR
//
