GenomeNet

Database: UniProt
Entry: A0A0W8CJ52_PHYNI
LinkDB: A0A0W8CJ52_PHYNI
Original site: A0A0W8CJ52_PHYNI 
ID   A0A0W8CJ52_PHYNI        Unreviewed;       880 AA.
AC   A0A0W8CJ52;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=AM587_10017433 {ECO:0000313|EMBL:KUF84110.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF84110.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF84110.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) 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:KUF84110.1}.
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; LNFO01002988; KUF84110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8CJ52; -.
DR   STRING; 4790.A0A0W8CJ52; -.
DR   EnsemblProtists; KUF84110; KUF84110; AM587_10017433.
DR   OMA; IRCTFDR; -.
DR   Proteomes; UP000052943; 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   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:SF9; KINESIN HEAVY CHAIN; 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:UP000052943}.
FT   DOMAIN          25..359
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          382..412
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        441..463
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..852
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         109..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   880 AA;  96260 MW;  9B69EC2A1F04728C CRC64;
     MDDGNSRRMT ANAPPPSLST PELASIKVFC RLRQQNQLEK REGAVQCSTV VGGRTMFLRN
     ERCEVDEIRC TFDHVFDIHS TQEEVYTHTA KPLVQDFLQG YNCTIFAYGQ TGSGKTHTIL
     GPKDGVLVSA DEEGGIISRV VKDLYEEVER AKTNPIELKV SFVEIYMEQI RDLLAPSGSS
     NTVGTPTNGG LKIRESAQHG VYIEEMTRVP SKSEAAMMEL VKSGTLSRAV SSTRMNKDSS
     RSHSILMISC VRPVSGRRAT MYIVDLAGSE LVNKTNASGR VLQEAKAINK SLSALSNVIK
     ALGEGKRHVP YRDSKLTRLL QDSLGGTAKT CLILAASCSS YNMAETISTL RFGLRAKEIK
     NPVVQRTDGD GGAGFAAGTI FKELYQRAME DMEAKNRKID ELQRLLTAKL QENQHPDDVE
     TAAATIEDSG KPQDTDGDHS SQDGDNEEDG DSAEEEGDEE ENDPAQSDAK KLELANQGLE
     EENKRLFGVL EALEKKLDEV TVDLSTGRPI LTLSSQRDSA TEGDCTSCGE SREGAAPSLK
     VWLESDNWRK SLESRTDTQG EDDLMQQLKQ RHSPEKPTPT SIAELEVVKA ASPVVIESLA
     LPSLQGTMPP CSTPDCVHHA DAEALSRQIV ELKLQLHYLS ENARLSLNGE SYSIVLENAR
     LKTRIEELEF QANLCNVACS QLEMKNRACE TRLSNQETHI GCLQNSLQEY QGLFKQQIIM
     SQEKCRLLTD ELEFYKKLAR CSQESYQHLG GSMSPGRRNK GKSPSPKKNN SSNSNGASNT
     PSLSALARDG AASSDSQHSW PSFTRTGSDI TLSPLTARAQ RFIVKPTGER ASSTAEQTPP
     AEASTSSQWH KTSVDLSLSL DELAQSATLP ASPVASPSFL
//
DBGET integrated database retrieval system