ID A0A225W3N5_9STRA Unreviewed; 1282 AA.
AC A0A225W3N5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kinesin {ECO:0000313|EMBL:OWZ12363.1};
GN ORFNames=PHMEG_00014492 {ECO:0000313|EMBL:OWZ12363.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ12363.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) 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 -!- 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:OWZ12363.1}.
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DR EMBL; NBNE01001869; OWZ12363.1; -; Genomic_DNA.
DR STRING; 4795.A0A225W3N5; -.
DR EnsemblProtists; OWZ12363; OWZ12363; PHMEG_00014492.
DR OrthoDB; 75571at2759; -.
DR Proteomes; UP000198211; 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 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:SF15; ZGC:66125; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000198211}.
FT DOMAIN 14..373
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 409..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 540..602
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 730..796
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 930..995
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1158..1221
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 409..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1282 AA; 143312 MW; 4758EFAFDC16DCBE CRC64;
MTTDSRERSE EQDSVKVCVR IRPLSSKEKY AQTKSCIRIA ASFDGLSTNN SASRDGVKGS
QQLIVGKDRA FTFDNVLGIN SSQTDTYRMC VAPLVQGFLD GYNATVLAYG QTGTGKTYTM
AGSGFDARGR EKNGELQGMI PRVINAIFKK LQQEGNNDNQ GRGECTLRVE YVEIYNEELR
DLLHPETTSK QLVIREDGEG NIVIAGVKSE LADSKEAVFR HLVVGGASRV TGSTMMNEQS
SRSHAIFSLL LEQRDIASST RRFSKFHLVD LAGSERAKRT GAVAGRFKES VSINQGLLAL
GNVISALGDD KRRVGTAAGT IHVPYRDSKL TRLLQDSLGG NARTLMIACV SPATINFEET
LNTLKYANRA KNIKNKPILN DRKESEEERL RNEEEILRMR KEISNLQTQL QQQKIATPPS
RTPSRPSWSV RKHTNTADQE RELAIASREL AQATTCVGMY GDAVENIRSY SMEAATQLVA
MEREIKSLGR PVQQRLNEIV KLLNESIKTA NCSVISAKKL LPSPNRSHDI DPECHENDQQ
EEETTLVQKL RRELNEAKAN LTRDEQIFEM KNADIQKLQA LLVEAKGKNE RLIDRVQELE
RGGQLWSNAK APGIEEEAKE HESENASTTT ISSPRGRSSQ WASTSKSKTP TSSRGLFTRR
ETTVYNSDDD KVVMGPPDED DIEEPRIPPA PRKSRSGSMM VFSRSSASRR GDYSRRSLNT
GSRLKTNEAI GKLEHTITAL QTKLEELQKK NEELLDAHED STRRWALDRQ NYECQLSDAE
HLIEALKRDN QVLEDSVLDD KRSEAKELAA TSSLSLNIRH SLSEKGTMTS MDQGRLDTSA
SSKSSQSPTT SSGTIGPVNK DAVLAAFESS VIQLVEYHAT RREVVYLLKG KKYAEQSRSE
AARRVNALEM QKMRHSLGVR ESISDLSKSL HALDERMLAE SKSIEELERL KKLKARAENK
LKGLRMKEEK AEFLNNEAQQ ELQDLEELLV DLDSHISFQD AELVAARNDL LAIKQRSESV
DAASPLHNLA NGLMQQLGLG SGDVSTSVMT KCLDEVARLR MRVSDMGSEV QELQGLLNER
EAALSQLESG LVVARDEFDR RLAAQQQESA VAMEQLKKMQ PKVLIPSNNE DNEETGDSHK
DIEWQKLIVR CQKKDEYIAD LEKHLVFYKS KAKQMQTQLQ QLIRSSSEQR PHKEEYDGDR
ELQLQRRVQQ LEDANDSLMK DLASAKVYLR TSKSRSNIVG TSGEHNGAKV VRISGSELRE
LPAPPAPLNA VEVHVRHFSE GE
//
