ID N1PXR5_DOTSN Unreviewed; 610 AA.
AC N1PXR5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=DOTSEDRAFT_69654 {ECO:0000313|EMBL:EME47788.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME47788.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME47788.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446536; EME47788.1; -; Genomic_DNA.
DR AlphaFoldDB; N1PXR5; -.
DR STRING; 675120.N1PXR5; -.
DR EnsemblFungi; EME47788; EME47788; DOTSEDRAFT_69654.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_2_3_1; -.
DR OMA; PRFYHHI; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000016933; 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 Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 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:UP000016933}.
FT DOMAIN 61..420
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..531
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 545..565
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 610 AA; 68667 MW; 7B9F10155CFC70DB CRC64;
MYNALRKRAA DELDQLCATF GSLLLTDMAA RASTASTPSL RSKTPVDMAR PFTPPDGDGG
NVKVVVRVRK FVKRELDKQS PCIIHMSPAT QETTIEPPEA TADSRKVLEE KKFTFDKSFW
SHNESDAHFA GQQDIYASFG EEFLDHNFDG YHTCIFAYGQ TGSGKSYTMM GSLDQPGLIP
RTCRGLFERI EAEQNGSITY NVHVSYFEIY NEHVKDLLTP RTNPPTYLKI RESKSDGVYV
QNLTDEPVKC YEDISRLMKT GDMNRTTAMT KMNDTSSRSH AVFTLTLKQI QHDLATDSTI
ERVARMRLVD LAGSERAGRT EATGQRLREG GNINQSLTTL GRVIAALADP KRQRATRMTG
LQNQPKRRAE VVPYRDSVLT WLLKDSLGGN SKTAMVACIS PTDYEETLST LRYADQAKRI
RTKAHVNQDA VSAAERDAKI MEMQEVIKQL QLSVNVSATR KRDEADRTQA ELEDYQRQVS
KMQRAMEESR AVSEVKIRAL TQEVDELRPQ NEALRIEIEA LRRHLALAVG ELKNPIVLPE
GFVEDDDGNS GDEYEEGDRD SGMGDDESDF ENRHGDWQAD VDDLLKDLGL FKRKVADDKM
RFPLPEQAGQ
//
