ID   A0A2G7G3Y3_9EURO        Unreviewed;       949 AA.
AC   A0A2G7G3Y3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=AARAC_003899 {ECO:0000313|EMBL:PIG87542.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG87542.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG87542.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG87542.1,
RC   ECO:0000313|Proteomes:UP000231358};
RA   Moore G., Beltz S.B., Mack B.M.;
RT   "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT   Aspergillus arachidicola.";
RL   Submitted (MAY-2017) 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:PIG87542.1}.
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DR   EMBL; NEXV01000151; PIG87542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G7G3Y3; -.
DR   STRING; 656916.A0A2G7G3Y3; -.
DR   OrthoDB; 5476186at2759; -.
DR   Proteomes; UP000231358; 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   CDD; cd01369; KISc_KHC_KIF5; 1.
DR   Gene3D; 1.10.287.1490; -; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF29; 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   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:UP000231358}.
FT   DOMAIN          34..357
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          402..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          670..739
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          775..892
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         115..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   949 AA;  105913 MW;  1BB2D7E39B55CC5D CRC64;
     MASSGPNSSN TSIKGAHILP ETDASVSSSI TDQFSVVVAR FRPQNKVELS SGGEPIVEFE
     NEQSCQISSK EGTGSFTFDR VFPMNSKQTD IFDFSIRPTV DDILNGYNGT VFAYGQTGAG
     KSYTMMGSDI DDDIGKGIIP RIVEQIFASI LTSPSNIEYT VRVSYMEIYM ERIRDLLVPQ
     NDNLPVHEEK SRGVYVKGLL EVYVSSVQEV YEVMRRGGTA RAVAATNMNQ ESSRSHSIFV
     ITVTQKNLET GSAKSGQLFL VDLAGSEKVG KTGASGQTLE EAKKINKSLS ALGMVINALT
     DGKSTHIPYR DSKLTRILQE SLGGNSRTTL IINCSPSSYN DAETISTLRF GVRAKAIKNK
     AKVNAELSPA ELKQLLRKAQ SQVTNFESYI SALETEVHVW RSGESVPKDR WTPGRNDVVS
     ATKAEARPRP STPSRLQEAR SETPRPDSRV GDRSSTPSLV LEKDEREEFL RRENELQDQI
     AEKESHIANV ERGLREAREE LRALKENSAR SGKDNEKLNT EVNELRMQLE KVSYESKEAA
     ITMDGLREAN SELTTELDDV KQQLLDVRMK AKETSAALDE KEKKKAEKMA KMMAGFDLGG
     NVFSDNERKL QDLINRVDTL HQISEAGETI APDDLLELRT SLSETQGLIR QAELTMNDRG
     ELSELQDSRR IEVEQKLADL ERDYEKLLER NLGEEDVEEI RERLEKVYVT RKDAEMQAAS
     ELRKEIAHKD EELSKLRQSL ADSQTRVSTN GAAGKNLQQQ IAEFDAMKKS LMRDLQNRCE
     RVVELEISLD DAREQYNNVL RSSNNRAQQK KMAFLERNLE QLTHVQRQLV EQNSSLKKEV
     AIAERKLIAR NERIASLESL LQESQEKLTQ ANHRFEAQLT AVKERLEAAK QGSTRGLPSM
     DSGGNFSFGG SRIAKPLRGG GGGSESSAPV AGVQSQETGK RTSWFFDRR
//