ID W2KRJ4_PHYPR Unreviewed; 741 AA.
AC W2KRJ4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=L917_13164 {ECO:0000313|EMBL:ETL87697.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL87697.1};
RN [1] {ECO:0000313|EMBL:ETL87697.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL87697.1};
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.
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; KI681029; ETL87697.1; -; Genomic_DNA.
DR AlphaFoldDB; W2KRJ4; -.
DR EnsemblProtists; ETL87697; ETL87697; L917_13164.
DR VEuPathDB; FungiDB:PPTG_03731; -.
DR Proteomes; UP000054423; 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; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 91..454
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 103..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 741 AA; 81112 MW; 784299892248D834 CRC64;
MGDDVEARSA PAAPPSTREL ASQLRASLSA LKRDVATSFR LCGRDFGILG AELVSALEGG
RQRERASADA LAHERTARVH LETRLAELQG NIRVLCRVRP MPATAAGSSG EESENTSPDK
RRKRVQVESA QELSVFSPVD GALYKSFSFS RVFHEQHSQL TVFKEVAPLV RSAVAGRHAC
VFAYGQTGAG KTHTMQGTES DMGLYYRAAE LIYSSITQQQ HVYDFKVRIQ IVEIYNEEIY
DLLAQNSSNS TTGTTSGDRG SPTSAGMGCH VGATSMCGNQ QSSSSSTLEI RHGENGVYLK
NVETIDAPST KEFHDAITRS KTKKNDRSNR AHTVLMIDIL RTSKANGETD TGRLVLVDLA
GSERLSKTAD TSALTVRESQ HINKSLAAVG DVLSALLAKE KHIPFRNSKL THLLQDSLFG
NANRTLLFVH VSPRSTDVNE TINSLKFASR VSHIQMGKSR RTERAEISRL NGVVANQVSQ
IQALQEKLTA ELELRKKYER RLEEYRQEEH RRRSKGEEAR KVLQQMRTPS PPELPPPISS
RRWSLFARKE KLANAQGLNG IENVAENILR GNESSPETAE IRISINGKPS GISPPTNFSR
RLSLSALDQR AAAPGLKTKA RDRSLPTQGK RKRSSTSEKV RSILKKQRVN DGGIIDLTEA
EADADNSTMA SKQVSFDLSL ETIGTSTASL PSREPAAATT PRIPVGGAVR VLASSRSVAA
PPVARRVASA KRIKQRPMGW R
//
