ID A0A2S6C2P9_9PEZI Unreviewed; 1048 AA.
AC A0A2S6C2P9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=CBER1_02992 {ECO:0000313|EMBL:PPJ53976.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ53976.1, 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:PPJ53976.1}.
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DR EMBL; PNEN01000572; PPJ53976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6C2P9; -.
DR STRING; 357750.A0A2S6C2P9; -.
DR OrthoDB; 453489at2759; -.
DR Proteomes; UP000237631; 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 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 InterPro; IPR031852; Vik1/Cik1_MT-bd.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16796; Microtub_bd; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000237631}.
FT DOMAIN 659..1040
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 583..645
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 752..759
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1048 AA; 115536 MW; 5E558059D769415E CRC64;
MEALENTRPS GLKPPSKLPA FAGTRALQET TLSEQNARTA DGASGIGSSM RPPSTIVPSK
HKVSNLPEPP MKRKTLAERA GEPANTLRNK PSISSGFGTR PTTSGANSFR APASIPSATG
SLRGLRPPSR QANGFGPGTR TNSNYSVTKT PAPRYDEDDD GDGTLSSRKG TPVLSFSSNA
LHVQKTRTKS NLHVRQHEPQ FQSARAKSQH SGSYFPSIGD DSSDGSSVAT SRNSSASSVS
APPQQIPITK GGPVGASQPS REVSLSTAFN TLSLTPKPRS SLRHRPSLER IKEELSPSKI
PKFACVANTS LRHTQSAQHL RSPSPNKHSI SAAGLQTPLT VTKTKRREQM PIFLTKEKLT
PVKGGWDTVD RLDHMERMFQ KLKGEMDSAN GAKDSIETSL EIFKTRCAEL EKEKNELKSD
LRITSTDLER TRNELHTTST DLRQVRRDHE REMLDVERKH ERELSDLRLK QEKQEIQFER
ERERSADKFR REMEEARRTW ERQQSDKEAD LTSQSWEEMA QLRADHEKEK AALQKEVDEL
RQAGESRATE SASEVQHLRD SSADMQKQLE ASKATEITLR SRISAFETRI AALEQERNTF
VEKAKFLEGN QEAQSLEFTS MHGKLEEAIA QKNEVLETLR KEEVLRRKLN NTILELRGNI
RVFVRTRPLL NGEDDPAKVE YLDQDSLEGC KEMVVHAPAT QSAMGTARNE KLPYAFDRIF
TPGTPNEDVF AECRDLVQSV VDGYNVSILS YGQTGSGKTY GMTGPRGIIP SAIKMLLSEM
QRLKTKGWEY AVEANFVEVY NETLNDLLGD AKSWDEGDGV AATSRGKTKE KHEIHHDPAT
GKTSVSNLTT IGLWPPPSND GSWPPAASVD GEEVDSSTNS YTEKAVENLL NTASSNRRVA
ATKANERSSR SHSVFILTLK GSCAATGETS EGVLNLVDLA GSERLKQSGA EGSRRKETQA
INKSLSSLGD VIAALGNKTS SEGHIPYRNS KLTYLLQSSL GGSTVGKSSR TLMLLHLSPL
QAHWQESKSS LKFAEKVHTT HIGTAKKR
//
