ID A0A024T9G2_9STRA Unreviewed; 952 AA.
AC A0A024T9G2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=H310_14602 {ECO:0000313|EMBL:ETV90644.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV90644.1};
RN [1] {ECO:0000313|EMBL:ETV90644.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV90644.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-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; KI914027; ETV90644.1; -; Genomic_DNA.
DR RefSeq; XP_008880714.1; XM_008882492.1.
DR AlphaFoldDB; A0A024T9G2; -.
DR STRING; 157072.A0A024T9G2; -.
DR EnsemblFungi; H310_14602-t26_1; H310_14602-t26_1-p1; H310_14602.
DR EnsemblProtists; ETV90644; ETV90644; H310_14602.
DR GeneID; 20091652; -.
DR VEuPathDB; FungiDB:H310_14602; -.
DR eggNOG; KOG4280; Eukaryota.
DR OrthoDB; 179133at2759; -.
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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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 11..392
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 44..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..455
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 524..617
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 487..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 952 AA; 107532 MW; 41D4984756AAD911 CRC64;
MSTVSGRYGS NFKVVIRVRP PLPRELQGDK PFQNVVSVDS SGHYLTVSDS SHHSSSSEDQ
QSNGSSSSSY SNHSFSFDHV YDQHSTQRAV YENTAKAVVE SSLEGYNATI FAYGQTGTGK
TYTMEGFNSS GGSLEDRGII PRAIEQIFMH IQANMSARMR FLVRASYLQI YNESISDLLK
PERNNLTIRE DKKRGVFVEG LSEWVVRSPE EIYGLMERGG AMRATGSTKM NEISSRSHAV
FIIIAEQSQT TYVDTAGKEI PPEEFTALVN TQARDRSKLE SLVRQSFKVG KLNLVDLAGS
ERVRLSGATG QRLEESKKIN QSLSALGNVI AALTDTRGRQ HIPYRDSKLT RILEDSLGGN
CKTTMMAMIS PALEAIVESL STLKFANRAK NIKNEARVNE DLDQKSLLRK YERELKRLRA
ELEEKNRNVV DKRRLLELDE QRRRAEEDKM AAIRALEQRS LEFMLEKEEK KKLEQRIIML
TSQMLMSHGK QKGANDDGSS NGGNGDGGEN EFSTEDPQFR IALKEQQDRI RKEYECRLAD
LEKERETIEE EKAQVDRYKQ LLLKQRDIMI ALTQRLNERD EQIMALQDEL DAYDRHQKSL
EEKLDEKTAQ LIHLQRVTME HNATSPNKNA ELIRALGDWG FKQTQQQRQS HPSLDPNGML
PAHLLTSHKQ FLPHEPLYNN NQLTKTPPKG LLLSADEKIQ ELQEVLATQG QELGRVTKEL
DEVRADKVSV EYVMRERLEK LVQAELEARL REHDQAALTK YQNRINELEV AHGTAAKLCG
AGRWAVRSPK NTHNLWIVGD LQGRCDTLTK ERKAVQTIME QKIKALVDAI ARASDATLET
VGGVDQIGEP AKWLCREVNA LQRLVNASIV ALRNANTDKA TGSTPPPTID KQPSGARVGY
SDFPPQQQSP QQLDTSKKPA LSSYVTGGLS VEELIQKRRQ QMQREKQQRQ HG
//
