ID A0A1S9DXK3_ASPOZ Unreviewed; 733 AA.
AC A0A1S9DXK3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=OAory_01023620 {ECO:0000313|EMBL:OOO13767.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO13767.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO13767.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO13767.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-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 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:OOO13767.1}.
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DR EMBL; MKZY01000001; OOO13767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DXK3; -.
DR VEuPathDB; FungiDB:AO090023000109; -.
DR VEuPathDB; FungiDB:AO090023000110; -.
DR eggNOG; KOG0239; Eukaryota.
DR Proteomes; UP000190312; 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; cd01366; KISc_C_terminal; 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; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000190312}.
FT DOMAIN 384..719
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 62..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 147..195
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 266..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 522..549
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 733 AA; 82886 MW; 9F0651E7A02A4EA1 CRC64;
MRKTQAFWGR ERVGDNFTLI PLISQFSQTR HYQEAYMHMS HKVGRELSGI LLKNMKGPTF
VPLGLNTPTT PTPSYKPLSP SKHSSKRKPP PVPQFLTKDS MITSFNCSTG AEWDQETREK
TMEEFFNAFV SRVSQAGQES FGLKETVELY KSRVNELEQS RKDLTEANLA LRVELESMKA
RIGTAEGALH DAQREHELAM DEFSSRQRLE VETVRADSKK KLDTIVAQHE DQLCELKRRF
ERELDDEKAS RLREINQLTS QTALDTQRSQ IELDRKDREI ASLQNDVQAL QQEIERERKS
TQGLRQNLDT ASSNSVTLES SIRALKARIE FLESGREEQS QAFERLNQQM MDALAETNAT
KDKLRKEETL RRKLHNQVQE LKGNIRVFCR VRPSLETEPQ TGIAQIQYPD ASEECKEINV
LGLEEKSSLG AVTKKNNNFA FDRVFGPSTQ NAEVFDEISQ LVQSALDGYN VCIFCYGQTG
SGKTYTMSSL DGMIPRAVHQ IYENATSLKE KGWRYTMEGN FVEVYNENLN DLLGKAEELD
KKKHEIRHDM QRGKTIITDV TTVRLDSPEM VENILKRAAA NRSVAATKAN ERSSRSHSVF
ILKLIGENDI TGERSEGTLN LVDLAGSERL SHSGATGERL RETQNINRSL SCLGDVIAAL
GQGKDGGHIP YRNSKLTYLL QFSLGGNSKT LMFVMVSPLQ AHLAETLTSL KFATKVHNTH
IGTAKRQARV RDC
//
