ID A0A0L1IXY2_ASPNO Unreviewed; 996 AA.
AC A0A0L1IXY2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=ANOM_007620 {ECO:0000313|EMBL:KNG84416.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG84416.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG84416.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG84416.1};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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 ECO:0000256|RuleBase:RU000394}.
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:KNG84416.1}.
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DR EMBL; JNOM01000209; KNG84416.1; -; Genomic_DNA.
DR RefSeq; XP_015405339.1; XM_015552876.1.
DR AlphaFoldDB; A0A0L1IXY2; -.
DR STRING; 1509407.A0A0L1IXY2; -.
DR GeneID; 26809424; -.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; PTHR24115:SF372; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 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:UP000037505}.
FT DOMAIN 9..379
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 680..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 717..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 996 AA; 109283 MW; B06A4F14A927ADFF CRC64;
MAIPSDASSI TVAVRVRPFT IREAAQISKC EDGPLFLGDG SLAGAPTPKL NQKGIRSIIK
VIDDRCLVFD PPEDNPVQKF SKSVVPNGKR VKDQTFAFDR IFDQNASQGE VYEATTRTLL
DSVLDGYNAT VFAYGATGCG KTHTITGTAQ QPGIIFMTMQ ELFERIDERS GEKATEISLS
YLEIYNETIR DLLVPGGSKG GLMLREDSNK SVSVSGLSSH HPQSVQQVMD MIMKGNECRT
MSPTEANATS SRSHAVLQIN VAQKDRNADV NEPHTMATLS IIDLAGSERA SATKNRGERL
FEGANINKSL LALGSCINAL CDPRKRNHVP YRNSKLTRLL KFALGGNCKT VMIVCVSPSS
QHFDETQNTL RYANRAKNIQ TKVTRNVFNV NRHVKDFLVK IDEQMNLINE LKAQQKDHER
IAFAKFKKQT EKKDAVVREG ISRIRNAYEH SLPERQERTA NMIKSRQISR RIGMLSSWIA
AFDSVCANSE HEEPLTNLQA IRKTAQGVLL ELESSRQHYH QRLSRSTWDR GINSAVEHAV
RQLQDFGIND NSDLANLHRE AELLKSNTER DAFSAVAEQE KGGEAETVQL LLQAQFEAIS
AIEDIMQMSE EEAVETGKNI LSKMLDSCST VTSSLVKPDG SLPPAQTFSP FKAMSPKPKK
RVSLAALPAG KTLAAPISLA PAAPASPGKG SPRRRRLGVG RKSVTFSPKK SQAKSTKRSV
RWKDDEQDGS LAEFQKTPQK PRAQLFPEAS KAVPTSPHCL ERHPPSYGSS PVPAPPEPTL
HVPKNNRFKA GFLSKKTSGS PIAPPPSTSL PASDGEHSPL RNIENSSFLN RAPIDRPSRI
AVRTSSGSYT SSPASDNKES WKANKDDAMR ISSAMRRISG GHFGAGASAN SLRVHRRRSP
GSATYGSSPP ENTMFTAQAR RMAKGEKEHE TKPGVLGPRN LPIMKNTGRR TTFGGDIRPR
DISLTSRDAI RLSAMATPIL QRPPESLYSN SGAGWR
//
