ID N1JIR6_BLUG1 Unreviewed; 993 AA.
AC N1JIR6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 28-JUN-2023, entry version 49.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=BGHDH14_bgh03560 {ECO:0000313|EMBL:CCU78085.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU78085.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU78085.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU78085.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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}.
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:CCU78085.1}.
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DR EMBL; CAUH01003951; CCU78085.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JIR6; -.
DR STRING; 546991.N1JIR6; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_21_1_1; -.
DR InParanoid; N1JIR6; -.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000015441; 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; cd01370; KISc_KIP3_like; 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:SF13; 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};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015441}.
FT DOMAIN 10..381
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 646..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 993 AA; 108631 MW; 5E9F77E8AFA7E7A1 CRC64;
MVFPDPGASS ISVTVRVRPF TINEAAQITK RDDGTLFLGD GSLAGAPTPK LGQKGIRPVV
KVIDDKCLIF DPPEDNPVTR FSRSVVSSMG KRVKDQTFGF DRVFDENTTQ AEVYESTARS
LLDSVLDGYN ATVFAYGATG CGKTHTITGT AQQPGIIFLT MQELFEKIAE RSDEKHTEVS
LSYLEIYNET IRDLLVPGGS KQGLMLREDA NQAVSVAGLS SHHPQDVQQV MDMIVSGNEY
RTVSPTAANA TSSRSHAVLQ INVAQKDRNA DVNEPHTMAT LSIIDLAGSE RASATKNRGE
RLLEGANINK SLLALGSCIN ALCDPRKRNH VPYRNSKLTR LLKFSLGGNC KTVMIVCVSP
SSAHFDETQN TLRYANRAKN IQTKVTRNVY NVNRHVKDFL VKIDEQMAMI NELKAQQKES
ETIAFSKFKK QTEKRDSIAR EGIARIRAAY DHSASERQEK LQNSKRLRQI ERRICLLSAW
VGAFEDVCAS REDEGMAPNL VSMRKTAASI IVDLESSRQH YQQLLTKTNW ERAVDSAYQN
SIRMLSEAGE CANGPDNSML ARETELLKYN AELEVANELL SLEKDSDRYE MRALLTAQVE
TIASLHDILG MSEDEAISHA RSILGRLLQS SSTTMSNIIK PDGSFKITDA IPPSKRGTPK
RKKHTRISDY KNAPAPIMQA LAAVAPHVYS SPVKFSPRRK KVGLGKKSVS FTPKKNHHQN
EFEKTPQKLA MTPEDPNIEE SYSLPALPTS PTPNAEVNDN DPLSSSPIPA APIPSIEIKS
KNRFQAGFLS RKSGGLSPSS IGQYSNEISP LQDIDACNIG NRSLQGNIQQ SFAEGSPNEC
EQSSGSEAEN SSRLIDQSDS LKIGKKLKRT GSLSRAGTSY DSSRTARRRS PTAVTSTASS
PPSENTLFTA GHARRMVSSQ REPALHSKVL SPRAASITKY GRRLTVDAGN PRTVSASLAG
GPIRVPSLNA ATLGNISKVR VSAIGDKSIS GWR
//