ID A0A1B8AJ08_FUSPO Unreviewed; 1352 AA.
AC A0A1B8AJ08;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPOA_06838 {ECO:0000313|EMBL:OBS20470.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS20470.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS20470.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS20470.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OBS20470.1}.
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DR EMBL; LYXU01000003; OBS20470.1; -; Genomic_DNA.
DR STRING; 36050.A0A1B8AJ08; -.
DR OMA; RHERINN; -.
DR Proteomes; UP000091967; Unassembled WGS sequence.
DR GO; GO:0005819; C:spindle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd20908; SUF4-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 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 InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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 SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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.
DR PROSITE; PS50808; ZF_BED; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 13..72
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT DOMAIN 42..70
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 328..699
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 118..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1352 AA; 147815 MW; 0129C4C4D51884CC CRC64;
MGKKRRGHPD IEEVLHRPWC YYCERDFEDL KLLISHQKAK HFKCDRCGRR LNTAGGLSVH
MNQVHKENLT QVENALPNRQ GLEVEIFGME GIPQEMLDQH RNRILQNFQQ AQKDRQIATG
NPLPGQGHQQ KKIKTESPDD LKQRLAEFRQ KKKEIAANGG VDPAAAAAAP AVTEPQDSFN
APPTYASQNP YEQPAFVQAP AAAVAPPYSF AANNLPARPS SGAALPTATG LPQRPTQGGA
WSGAPAAGDD IDNLIRMAEA GIKPAAPAED GDKKKKEKKA RMFYDDAEIS PEERMAALPS
SRLQQHRITS NDEIMAITAA PSAAGQSSIT VAVRVRPFTI REASQLQKNN DGTVFLGDGS
LAAAPTPKLH QRGIRNVIKV VDDRCLVFDP PEDNPVQKFG RSVVPSSKKV KDQVFAFDRV
FDDNTTQSEV YEGTTRTLLD SVLDGYNATV FAYGATGCGK THTITGTAQH PGIIFMTMQE
LFEKIGERSQ DKVTELSLSY LEIYNETIRD LLVPGGGGKA GLTLREDSNA AVSVSGLTSH
HPKDVQEVMD MIVQGNEYRT VSPTEANLTS SRSHAVLQIN VAQKDRSAGT NEPHTMATLS
IIDLAGSERA SVTKNRGERL VEGANINKSL LALGSCINAL CDRRQKQHVP YRNSKLTRLL
KFSLGGNCKT VMIVCVSPSS AHFDETQNTL RYANRAKNIQ TKVTRNVFNV NRHVKDFLVK
IDEQMALINE LKAQQKNAEG MFFAKFRKQA EKRDALAREG IQRLRTAYEH SATERHERIN
NMKRLKGFER RIGMLSGWIA AFDTVCDQRG DEDSMPQNLV AIRKTAQGIL VELENSRHHI
HQKLEKSGWE RAIDTALSHT LQQLQGTDGA DSGETDKLTR EAELLKANFN REAYREVLEQ
DKAGDAAMVQ MLLTAQFDIL ASLHDTLEMG EEEAVAHAKE SINRLLQTGF TAAGQVVKPD
GSMPVIEVFS PRKRGTPKRK KAIAMHIKPV SAPVFMPENT PVSPTKGSPR RRRVLGASKK
SISFTPVKMM KKKGGVRWRD DETEEGTLVD FSQTPQKFNS SPAMPSPEKD IVAPPMPSYL
EPDESKIDES KIEDSTDSSP RLEVPEVSSL GGAKPSRFQA GFLSKGARPS LAGGSPQAPS
LSLRLGSVSP DVQRTPPLRS LDVTKSGNFS PSPSGLGIPR PIRHFNRVHD ENNPPGSGSD
SETSTIDARK LQTALRTAMK EKARRASILA GTGASSSKRV SSMGMLPERS APRPSLSGPL
ASTTNGISRL RRGSAERRRS PPMACFANDF TIDRALTQGQ ARRMNLSTTR ASEVNGGSPQ
GSMAGGTARR ITIGTGSGAA HRRQVSAGGT WR
//
