ID A0A0W8CD95_PHYNI Unreviewed; 1044 AA.
AC A0A0W8CD95;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Kinesin protein {ECO:0000313|EMBL:KUF81982.1};
GN ORFNames=AM587_10013603 {ECO:0000313|EMBL:KUF81982.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF81982.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF81982.1, 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 -!- 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:KUF81982.1}.
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DR EMBL; LNFO01003882; KUF81982.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8CD95; -.
DR EnsemblProtists; KUF81982; KUF81982; AM587_10013603.
DR OMA; EQIFCHI; -.
DR Proteomes; UP000052943; 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; 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:SF29; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 2.
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:UP000052943}.
FT DOMAIN 100..502
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..600
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 626..719
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 796..888
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 976..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1044 AA; 116309 MW; 7B76CABF67726FB6 CRC64;
MSINVSSAWS SPSSSARSSP LSTSSPSNTR RQQHYSSPAA GGYLQRTAIS NAYNSGTARS
EDGETASTTS EGFLERPSSP AHSTHSISSS SSRFGERGSN FKVVIRVRPP LPRELHGDRP
FQNVINVDQH GHVLTVSENL SALSSSGSVD SDSSTPGAYG SHVFSFDHVY DQQCTQSTVY
ENTAKAVVES SLEGYNATIF AYGQTGTGKT YTMEGFNSGS GSVEERGIIP RAIEQIFCHI
QANVSARCRF LVRASYLQIY NESISDLLKP ERSNLTIRED RRRGVFVEGL SEWVVRSPEE
IYGLMERGGA MRATGSTKMN ELSSRSHAVF IIIAEQSKTT YVDSKGNDVA PEEFMALVNA
YQARHGNTPT NGKAPNGANG NAAALHPKLE AMVRQSFKVG KLNLVDLAGS ERVRLSGATG
QRLEESKKIN QSLSALGNVI SALTDARGRQ HIPYRDSKLT RILEDSLGGN CKTTMMAMVS
PALEAMTESL STLKFANRAK HIKNEARVNE DLDQKSLLRK YERELKRLRA ELEERSRNVV
DKRRLLELDE QRRRAEEDKM AAIRALEERS REFMREKEEK KRLEQRISAL TSQMLMSNQR
RLTPTSLSGD GETLNVEDPL IRDALKEHQD RIRQEYECRL ADLEKERETI EEEKAQVDRY
KQLLLKQRDI MIALTQRLNE RDEQITALQD ELDAYDRHQK ELEEKLDEKT AHLIHLQRVA
MEHNASSPGK TDAELLKALG DWGGGATQAK MAPTVVSAVS EPPAELLITH KQFRPHPVDP
VIINDNNYSN NTGNGLLSAE EKIKELRALV DAQTAEHQRM AKELEDVKSE KVSVEXQMRE
KLEKLVQVEL EARTKDLNRS DNRDKQQLAN LQRQLEKMML ENQQLQTRTV TDDQTQLQAR
CETLVKERRA VQTIMEHKIK ALVTAIGEAS DATLQTAGGA DKLGEPAKWL AREINALQRL
VNASIVALRN ADAGNGKPTK ESSSSQPTPT TAPAGISSNR EKTDASRTMV SSISGAQPTN
LSVDELIDQR RAQLQQQRER YPSI
//
