ID G4ZL75_PHYSP Unreviewed; 1110 AA.
AC G4ZL75;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Kinesin-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYSODRAFT_508410 {ECO:0000313|EMBL:EGZ15589.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ15589.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ15589.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ15589.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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}.
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DR EMBL; JH159155; EGZ15589.1; -; Genomic_DNA.
DR RefSeq; XP_009529338.1; XM_009531043.1.
DR AlphaFoldDB; G4ZL75; -.
DR STRING; 1094619.G4ZL75; -.
DR EnsemblProtists; EGZ15589; EGZ15589; PHYSODRAFT_508410.
DR GeneID; 20658864; -.
DR KEGG; psoj:PHYSODRAFT_508410; -.
DR InParanoid; G4ZL75; -.
DR OMA; NAWETLC; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
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; cd00201; WW; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1470.10; Photosystem I PsaD, reaction center subunit II; 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 InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00397; WW; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_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 Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT DOMAIN 152..186
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 718..1060
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 312..367
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 403..564
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 609..689
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 811..818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1110 AA; 122732 MW; 2AE3FE839B32C02E CRC64;
MAEEQHLSRI AQSSPRGGVS ARSSVTYSGR QVPLVDLAFQ GGDVSEPPVK MPSSRARFQQ
EDEYVAPSTS RVASGEGIPV SALPRAAASW HAGNGSAASY KSLPLAQDES AMMEASDPAL
FHAAVEEHAR RLGIEPTVDG EFLWIARESL VAPLPDGWYH VTATETGQPY YYNEISGESR
WDHPSDDQFR QLFREMKQKQ MKAHAFRDPH PARYYDAGGG YQSGVAWQEN EQDHRQMQYA
AQSQQGWDRR QAQGYYQGYE TPYKAPQAQV YSPRGDEGDR NYPVADSEST PVSTGRQQNG
TPRGDSQLAR KLQEMEEQKT KDEEVITGMK TEVADLKRQL ASRDQALEAL KSEVGQVNEN
LGDLTQQMEE RTKERDEIVV ANQTLKRELS LARSGMEGST KAHEELLEEH QAVIKELSLA
KAKLKEVQLK QRGEAEDVES LQAQLSGEQT ARAQMEQQLE QATKEQSAMA RKFEAAQATI
RRLQEDLSRK RETEEKENGE AVAAAAEAAA TAAATIKAIG DQLADKEREL EAERARAFSL
QQEIEQLRSS QAEAKDTLEQ DLQKQLGDSV AETRKELEAA KVSLTSTMAE KVAVGKQFEE
YKITSAAQIS ELEDQQRTLK REFRAMEREF KTQQGLSKER EDELASLKLA LESAETKLSS
VAQTIQRERM EAFAEAQQAS AEIARQANEE KARVADLYTQ EMLARRKLHN RLMELQGNIR
VFCRVRPIQP VELKSEQSAL AVFFRENDHE SLDLFVGSEA GDKANQIGQK HAFEFDHVFQ
PNSTQEQVFE QTRALVVSAL DGFNVCIFAY GQTGSGKTHT MEGPENDRGV NFRALRELFS
IRDDRMAAGN FECSLKLSIL EVYNETIVDL LEGGGRAPGA ASPAAVKGLD VRVGKTGVYV
ENLIEVEVFN EGDVLDLMRL GHSHRSVGSH DFNEHSSRSH LVLSITLETG MKTDARRRTS
KLHLIDLAGS ERVSKTAASG QRLKEAQNIN RSLSALGDVI AALGANSKHV PYRNSKLTFL
LQDSLSGNSK VLMFVNVSPV QWNAWETLCS LNFASRCRSV ALGQAKAATA TASGAPTQGN
GMQATMSMSA MIPSSNGGTR APGTRPVPSR
//
