ID A0A0C4DQN1_MAGP6 Unreviewed; 2032 AA.
AC A0A0C4DQN1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Myosin type II heavy chain {ECO:0000313|EMBL:KLU83108.1};
GN ORFNames=MAPG_02174 {ECO:0000313|EMBL:KLU83108.1};
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_02174T0, 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:KLU83108.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU83108.1};
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:KLU83108.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU83108.1};
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_02174T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_02174T0};
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_02174T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_02174T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; ADBL01000552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADBL01000553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876967; KLU83108.1; -; Genomic_DNA.
DR SMR; A0A0C4DQN1; -.
DR STRING; 644358.A0A0C4DQN1; -.
DR EnsemblFungi; MAPG_02174T0; MAPG_02174T0; MAPG_02174.
DR VEuPathDB; FungiDB:MAPG_02174; -.
DR eggNOG; KOG0161; Eukaryota.
DR OMA; QRAMDIE; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000011715; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000011715}.
FT DOMAIN 127..177
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 181..875
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..775
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1646..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 953..1159
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1188..1540
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1945..2021
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2032 AA; 231430 MW; F99AC794CB719ECB CRC64;
MSGLNGTGLR NNPFMRNASP SAAPGSTPAP RSRPKSVSFP SPSPLSGLST PTSGSPHVRN
NSQAVIAGAM GGNAGSSGSI PRHSREGSGR GSTPSSNTFA PSFIKSEEMQ RRPVDVVRGI
EGENDFSGKR YVWLKDPQTA FVKGWVVEEL GSGRLLVQCD DGSQREVDAE TVDKVNPAKF
DKAGDMAELT HLNEASVVHN LYTRYQSDLI YTYSGLFLVT VNPYCSLPIY TNEYINMYKG
RSREDTKPHI FAMADEAFRN LVEEGVNQSI LVTGESGAGK TENTKKVIQY LAAVAHSDHG
KGGKGHQSNL SAQILRANPI LEAFGNAQTV RNNNSSRFGK FIRIEFSKGG SIAGAFIDWY
LLEKSRVVRI NAHERNYHVF YQLLKGADRR MKQDFLLDNM DCEHFAYTRD GNDTISGVSD
REEWETLMEA FEVMGFSAAD QSAVLRTVAA VLHLGNITVV KESRAADQAR LAPDAKEHAE
RVCQLLGVPL EPFLQGLLHP KVKAGREWVE KVQTPEQVRL GLDALSKGIY ERGFGDLVTR
INRQLDRTGM GMDDSRFIGV LDIAGFEIFE ENSFEQLCIN YTNEKLQQFF NHHMFVLEQE
EYAREQIEWQ FIDFGRDLQP TIDLIELPNP IGVFSCLDED CVMPKATDKT FTEKLHALWD
KKSDKYRPSR LRHGFVLTHY AAEVEYSTDG WLEKNKDPLN DNITRLLAAS TDAHVANLFG
DCAADQDDDS GGMRSRVKKG LFRTVAQRHK EQLSSLMAQL HSTHPHFVRC ILPNHKKRPK
QFNNLLVLDQ LRCNGVLEGI RIARTGFPNR LSFAEFRQRY EVLCRDDMPR GYLEGQAATS
IILSKLGLDK GLFRLGLTKV FFRAGVLAEL EEQRDALITE IMIRFQSLAR GYIQRRIAYK
RLYRAEATRV IQRNFQVYLD MCENPWWQLL VRMKPLLGAT RTATEVKRRD EMIRQLHEQM
RQEEAHRARL EEERRNCHAD MVRIQQTLES ERALALDKEE IFKRLQSREA ELEEKLAGAI
EDQERLEDQL DSLLDAKKQA EEEVEKYRSQ LEQAATLMSK LEDEKRELAA RVTALEAEMQ
DMSQQQSQRS VQEEALQDEI KMLQSQLSLK DRKARDLEGK LLKIDQDAEV KLAAAQKELQ
AAKARETRLT TENSDVKQQL TQLSQTSTDY EDLVRKKESE LVILRGDNKK FEMERRSLDE
QMKTLSAEKE KASGRLREVQ AEISALKSQQ SQLQREAEDA KNLLEARLSE DAQADQNRQV
LEGQIKDLKE ELYKAQMDLS RERQSRDDVL LLGEHKYNTL QEEYDRLNES KITIEKELYA
QQDTLRRTME ARTTAERERD EAREEIRRLR AAKLQAEEAR REAESAGERA ALKIARERET
SLSKDLDAAQ QRLQWFEEEC AKLNHQVEDL NKLILESGEF GLKNDQEKER MQRELHTVKS
RLTASENDNR ALLNKLQQKG LEIARSTSRA SEASRGQVQM LQREKARLDE QNAKLNKQLG
DAQLTIASLE KKAEKLQLNL EDLNHEVARE VKASRNAEKA SSGFTAQLAE ANRTIESERT
LKTQAQTTVR TLQGTLDARD KELADLRTQL LSILKTVEPE PDLQPDCGHD RLVSKSFDLA
RKVEELQQSL RVQTAARASA EAQVSELRAA AQQSDRLDST RPKLEEMDPN EAPFNASPTH
RKSKVNGRHY SNVSTPPRRF NNPDHDPAHD SIRSDRTADV LSFNNRQDLK AEIEELQNRL
QLAEIKNRHL ESQLERATPG PDAVNGDDSP SIRRRAEKLE KANSRLQEML DDSTKKVSVL
EKAVRTGELS LRDIQTRSHE EILDVLNSQE ESRRSLLHSH RDAVAELADI RDHFDRMRHE
RAKLEVDLRD ARSDLQDMAL ARDQEAASRS QLLQEFSDLQ IRLDAEASKL GDVTASLNLY
KSRADEYFSK LEQAEIAVLK ASRAEQFARA QAREAEETCA EALTERKRMD ATLEDLQRQN
QRLEERVEDM STDLEAATQA KRRLQHELED YRAQRANDIE DKEVPSLTKG FL
//
