ID A0A0C4DPC6_MAGP6 Unreviewed; 1215 AA.
AC A0A0C4DPC6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Kinesin-II 85 kDa subunit {ECO:0000313|EMBL:KLU82619.1};
GN ORFNames=MAPG_01690 {ECO:0000313|EMBL:KLU82619.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_01690T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KLU82619.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82619.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU82619.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82619.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_01690T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_01690T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_01690T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_01690T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000256|ARBA:ARBA00034704}.
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DR EMBL; ADBL01000411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876966; KLU82619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4DPC6; -.
DR STRING; 644358.A0A0C4DPC6; -.
DR EnsemblFungi; MAPG_01690T0; MAPG_01690T0; MAPG_01690.
DR VEuPathDB; FungiDB:MAPG_01690; -.
DR eggNOG; KOG0243; Eukaryota.
DR OMA; DWETFDQ; -.
DR OrthoDB; 536293at2759; -.
DR Proteomes; UP000011715; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IEA:UniProt.
DR CDD; cd01364; KISc_BimC_Eg5; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR047149; KIF11-like.
DR InterPro; IPR047241; KIF11-like_kin_motor_dom.
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; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR PANTHER; PTHR47970:SF12; KINESIN-LIKE PROTEIN KIF11; 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 Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000011715}.
FT DOMAIN 101..444
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 688..715
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1165..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1215 AA; 132713 MW; 1F7ABA812AAE775F CRC64;
MSSTREPPRR RAAGASTSGL PGPSTTRSGA IGRAGSRLGV RSSIAPARNV RHGSVVASRI
DRAGAVSPTG SVSSIATTGT KRKERDFDSE AGVGDEVVGT NINVVVRCRG RNGREVQENS
AVVVSTTGVK GTVVDLSMGP NALSNKTYNF DRVYSSAADQ SMIFDDTVKP ILDEMLSGYN
CTIFAYGQTG TGKTYTMTGD MHESMGILSD AAGIIPRVLQ ALFNKLEMEE SDNCVRCSFI
ELYNEELRDL LSADDSAKLR IYDDNSRKGH STTVVQGMEE RHITSAAEGI KRLQEGSVRR
QVAATKCNDL SSRSHTVFTI TVYVKRPGEN GEDYVSAGKL NLVDLAGSEN IQRSGAENKR
AAEAGLINKS LLTLGRVINA LVDRSAQGDK NHHIPYRESK LTRLLQDSLG GQTKTCIIAT
ISPAKSNLEE TISTLDYAFR AKNIRNKPQI KTIMSKHSLL RDFTAEIEKL RGELVTTRQR
NGVYLSNESY EELTVQNESR RILTEEQSAK IETMETNLRN KVQELFDLTS SFMGLKKENE
GTKAQLDDTK EVLDQTELVL AATRKALGDE TQLRKAHQET EEKLAALGSE LIGTLDRTVR
DVSGLRAKNK RKSDLQNLNR STWATSQDQV ADVTEMVEGR IQEFKQDQEE HISSISQRVE
SFVQAELQKL SETQAFLDEH LGRFAISKKE LLEHKEQSKQ EMDAVLDEIK VVRDTIKERV
GESLQVIAGA AERIAADVLS ELSQFHSQLQ SSYSSLGKDF KSMFDDLSKT LISQRSESDN
LRRQLEGAGE SLIQSNAHAS SRIQEIMAEE RRQAAEERKL LLAQITLLIN NQGEEQETRL
AAKASQISQD MLSSTAAFEG SVVQYSEGMG VWGIKDSEMQ SEVGKSKETL NTKVGDDWNI
ANKHSTSIQA TTKSIHAETV RVVDEQMRDL DVQMQDLDSF VTRARSQNAT HLSQDAGAVQ
QLSQAVEASY GDLSARFKDG FERIKDVGEE LVADHGELQE ALEPLDDNVC RPLSNLRDTI
SKTILQEYQP TGDTPEKTQY LYPKELPRTA IPASQLARLI DEDMPASTPS KSAPSIFNDL
DSDASGILRP GSPAASPTMS GSINTNNQAR HPLGMSLREV NPNLAAAGGI HFNAAASTLS
LGSGLASASA NAKEGDGQIQ PMFRRSARSA SGTQSKGGAN VKIPGSKTAS LGVENMPPSS
ALSQSMSRRK SPRLH
//
