ID A0A024G020_9STRA Unreviewed; 866 AA.
AC A0A024G020;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=BN9_009860 {ECO:0000313|EMBL:CCI40202.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI40202.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI40202.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI40202.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI40202.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAIX01000006; CCI40202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024G020; -.
DR STRING; 65357.A0A024G020; -.
DR InParanoid; A0A024G020; -.
DR OrthoDB; 179133at2759; -.
DR Proteomes; UP000053237; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 1.
DR Pfam; PF00225; Kinesin; 2.
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:UP000053237}.
FT DOMAIN 81..472
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 598..691
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 729..756
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 866 AA; 98525 MW; 9615852364E0B0B6 CRC64;
MEYTSRKPLH STSRSRSALH SHGNDPSPLR TKAIRKRTSQ PQYPQTHINY IASSPAHSNR
SEHDSDAIST HSSTSSERGG NFKVVIRVRP PLPRELESDR PFQNVIQVDS SGHLLTVTEN
SMPTGMDPSN MAMYGSQVFS FDHVYDQHCT QSTVYENTAK AVVESSLEGY NATIFAYGQT
GTGKTYTMEG FNSAGLVEER GIIPRAIEQI FQHISSNVSA RTRFLVRASY LQIYNETISD
LLKPERNNLT IREDKKRGVF VEGLSEWVVR SPEEIYGLME RGGAMRATGS TRMNEMSSRS
HAVFIIIAEQ SRTSYVDTQG NELSPEEFTS LVNAYQSRLG PNKLGKHAQG RLQRGHPSIE
SMIRQSFKVG KLNLVDLAGS ERVRLSGATG QRLEESKKIN QSLSALGNVI AALTDFRGRQ
HIPYRDSKLT RILEDSLGGN CKTTMMAMIS PAQEAMIESL STLKFANRAK NIKNEARVNE
DFDQKSLLRK YERELKRLRA ELEEKSRNVV DKRRLLELEE QRRRAEEDKM AAIRALEERS
KEFMKEKEEK KKLEERITML MSQMLMSSHH ETLQFGNNEE INVFAGNVED PIVRDAIKEH
QERIRKEYDC RLADLEKERE TIEEEKAQVD RYKQLLLKQR DIMIALTQRL NERDEQITTL
QDELDAYDHH QKELEEKLDE KTAHLIHLER LAMEQGTPDS ISDTHLEPQS VVTEANDTKR
MEHSIAEETE KLKLRIACLE NEKNALQQTN ESQTNCAEEK VNGLVEQCET LLKERRAVQT
IMEQKIKALT NAIGEASAAT LQTAGGVKQL GEPAKWLLRE VNALQRLVNA SIIALRNAER
STKPALWEQD SSQRKHTSVR PVEPSN
//
