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Database: UniProt
Entry: W2JDP9_PHYPR
LinkDB: W2JDP9_PHYPR
Original site: W2JDP9_PHYPR 
ID   W2JDP9_PHYPR            Unreviewed;       621 AA.
AC   W2JDP9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=L914_05739 {ECO:0000313|EMBL:ETM50177.1}, L916_05727
GN   {ECO:0000313|EMBL:ETL43857.1}, L917_05614
GN   {ECO:0000313|EMBL:ETL97029.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL43857.1, ECO:0000313|Proteomes:UP000053864};
RN   [1] {ECO:0000313|EMBL:ETL97029.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL97029.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETL43857.1, ECO:0000313|Proteomes:UP000053864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL43857.1,
RC   ECO:0000313|Proteomes:UP000053864};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ05E6.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETM50177.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM50177.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica IAC_01/95.";
RL   Submitted (NOV-2013) 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}.
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DR   EMBL; KI672080; ETL43857.1; -; Genomic_DNA.
DR   EMBL; KI678799; ETL97029.1; -; Genomic_DNA.
DR   EMBL; KI692055; ETM50177.1; -; Genomic_DNA.
DR   EnsemblProtists; ETL43857; ETL43857; L916_05727.
DR   EnsemblProtists; ETL97029; ETL97029; L917_05614.
DR   EnsemblProtists; ETM50177; ETM50177; L914_05739.
DR   VEuPathDB; FungiDB:PPTG_02079; -.
DR   Proteomes; UP000053864; Unassembled WGS sequence.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   Proteomes; UP000054532; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF33; KINESIN-LIKE PROTEIN; 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}.
FT   DOMAIN          80..452
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          546..618
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   621 AA;  68381 MW;  8E8977579869BBE0 CRC64;
     MIAAAPPRGA RRIRRLRSPS VTASRRPPGL PPVQRQRTPE VPSPRVERSP RRLADYGTTD
     LSVISEAGQG DIKSKGRADT VRVVVRCRPM SAAERARGDQ SVFRFPPKQP TTLQVVSTQN
     SSSSSNNSSG SARELVRSFQ FDLCASEELS QRQFFRTCGV IPLLESVVEG YLATVFAYGQ
     TGSGKTYSMS GLNELLAGTE LRNEGMGDSN AMDLSDGLIP RSLKHLFSLL DQAPIDVKTV
     VRASYCEIYN EQVFDLLNPG SGALNMRWNA RAGFYVQDLL VVRCDSLSDV LAVVAEGHRN
     RHVASHSMNA DSSRSHSLLT VHVDRTEVRD SDVGKSHGVT RYGKMSFVDL AGSERLKETK
     SSNTEETSNI NRSLLTLGKV ISALASSSGG GSATTTSNGN FIPYRDSKLT KLLMDSLGGQ
     SLTLMIACVS PSATALEDTL NTLHYATRAK NIRNKPAVQV DPVELELSNL RHENHVLRAE
     NHALRLRLQL AGPMLNQHTS QPQQQSSLVS VPSNSRLLPL NNTSLSPRGA MKPSLSSVSP
     SRHNQLQVLQ DDHDKLTQRA AVAEQRLKEI EAENRTLRQR QNGTSSPNNE IRQLREQVQQ
     LQQREQELMQ ALSRRSRRET H
//
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