ID A0A067PPR9_9AGAM Unreviewed; 739 AA.
AC A0A067PPR9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=JAAARDRAFT_137340 {ECO:0000313|EMBL:KDQ53292.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ53292.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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}.
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DR EMBL; KL197734; KDQ53292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067PPR9; -.
DR STRING; 933084.A0A067PPR9; -.
DR HOGENOM; CLU_001485_27_0_1; -.
DR InParanoid; A0A067PPR9; -.
DR OrthoDB; 129693at2759; -.
DR Proteomes; UP000027265; 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; cd00106; KISc; 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:SF1000; KINESIN-LIKE PROTEIN KIF22; 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:UP000027265}.
FT DOMAIN 4..327
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 367..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 503..537
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 446..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 739 AA; 80265 MW; 67BCDBFF1DC4D246 CRC64;
MAHKVKIAAR LRPRLAGELE DDSIHIIKET GGSAICVTNP RDSSQVFKFP FTSCYDQSST
QEEIFDKDVK PLIDVVFSGV TVTIFAYGVT SSGKTHTMQG TKSDQGVIPR VVRSLFSKRA
HLPPNQTIAF TVSYIEIYKD EVYDLLVNRD NAPKLPVREN DAGQVFVANL TKTEIGSVQE
FDGLYSRATK HRSVGATNLN RASSRSHAVL TIEVAIGDLA SDMTLTGKIN LVDLAGSENN
KLTGNDASRM AESAAINKSL SVLGQVVHAL NQGASRIPYR DSKLTRLLQD ALGGSAVGLL
ICNLAPGMKF RQDTLNTLNF AVRTKNVENK PVVNERDNRP APKLHFAALA PSAPKLAPAG
VALGGGGGGG ASRPSLVPRQ SIAPRIGGGV GPSRMPRGSM VGAGGSGYQN FAVAGAGMGK
GIGGISEEDI DARIAKMVEN EVTRRLEEKE RERADKAKAE EERRVKEQEL QQREEVRSST
PPAVQSEGSS QTLLPSGVLT PLLKRHEDLD VELRSRLQEL EKKFERDNKE IRLADVLSPV
SRKKTGRAYV ALARAHSDKG DLHVALELYR KASTYVTDNV KLQERIIEIE WAVKNGKDFR
PSPKRSKKNK SKKRERSKGL EGESSSTSTL HSSSHNMTGG TSLETHFEEP EGAMEIDEES
EVMDMVVVQG DHQGQGRSQV RFGSELTNRG DGGDESRVGT PAKKTRSGKG KRKSAEVVSD
DEWEPPAPVK RGKRKLAVS
//
